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Volumn 74, Issue 2, 2011, Pages 316-345

Liquid chromatography and mass spectrometry in food allergen detection

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGEN;

EID: 79951659609     PISSN: 0362028X     EISSN: None     Source Type: Journal    
DOI: 10.4315/0362-028X.JFP-10-336     Document Type: Review
Times cited : (63)

References (369)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • Aebersold, R., and M. Mann. 2003. Mass spectrometry-based proteomics. Nature 422:198-207. (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 22744441541 scopus 로고    scopus 로고
    • Proteomics of gluten: Mapping of the 1Bx7 glutenin subunit in Chinese Spring cultivar by matrix-assisted laser desorption/ionization
    • DOI 10.1002/rcm.2032
    • Alberghina, G., R. Cozzolino, S. Fisiichella, D. Garozzo, and A. Savarino. 2005. Proteomics of gluten: mapping of the 1Bx7 glutenin subunit in Chinese Spring cultivar by matrix-assisted laser desorption/ionization. Rapid Commun. Mass Spectrom. 19:2069-2074. (Pubitemid 41026432)
    • (2005) Rapid Communications in Mass Spectrometry , vol.19 , Issue.14 , pp. 2069-2074
    • Alberghina, G.1    Cozzolino, R.2    Fisichella, S.3    Garozzo, D.4    Savarino, A.5
  • 3
    • 56749178804 scopus 로고    scopus 로고
    • High level expression, purification and physico-and immunochemical characterisation of recombinant Pen a 1: A major allergen of shrimp
    • Albrecht, M., S. Alessandri, A. Conti, A. Reuter, I. Lauer, S. Vieths, and G. Reese. 2008. High level expression, purification and physico-and immunochemical characterisation of recombinant Pen a 1: a major allergen of shrimp. Mol. Nutr. Food Res. 52(Suppl. 2):S186-S195.
    • (2008) Mol. Nutr. Food Res. , vol.52 , Issue.SUPPL. 2
    • Albrecht, M.1    Alessandri, S.2    Conti, A.3    Reuter, A.4    Lauer, I.5    Vieths, S.6    Reese, G.7
  • 4
    • 0032125079 scopus 로고    scopus 로고
    • Identification of peptides in Cheddar cheese by electrospray ionization mass spectrometry
    • DOI 10.1016/S0958-6946(98)00097-1, PII S0958694698000971
    • Alli, I., M. Okoniewska, B. F. Gibbs, and Y. Konishi. 1998. Identification of peptides in Cheddar cheese by electrospray ionization mass spectrometry. Int. Dairy J. 8:643-649. (Pubitemid 28548039)
    • (1998) International Dairy Journal , vol.8 , Issue.7 , pp. 643-649
    • Alli, I.1    Okoniewska, M.2    Gibbs, B.F.3    Konishi, Y.4
  • 5
    • 0034730929 scopus 로고    scopus 로고
    • Applications of mass spectrometry to food proteins and peptides
    • DOI 10.1016/S0021-9673(00)00745-7, PII S0021967300007457
    • Alomirah, H. F., I. Alli, and Y. Konishi. 2000. Applications of mass spectrometry to food proteins and peptides. J. Chromatogr. A 893: 1-21. (Pubitemid 30657889)
    • (2000) Journal of Chromatography A , vol.893 , Issue.1 , pp. 1-21
    • Alomirah, H.F.1    Alli, I.2    Konishi, Y.3
  • 6
    • 57149087037 scopus 로고    scopus 로고
    • Expression of globulin-2, a member of the cupin superfamily of proteins with similarity to known food allergens, is increased under high temperature regimen during wheat grain development
    • Altenbach, S. B., C. K. Tanaka, W. J. Hurkman, and W. H. Vensel. 2009. Expression of globulin-2, a member of the cupin superfamily of proteins with similarity to known food allergens, is increased under high temperature regimen during wheat grain development. J. Cereal Sci. 49:47-54.
    • (2009) J. Cereal Sci. , vol.49 , pp. 47-54
    • Altenbach, S.B.1    Tanaka, C.K.2    Hurkman, W.J.3    Vensel, W.H.4
  • 7
    • 4644231740 scopus 로고    scopus 로고
    • Characterization of a calcium-soluble protein fraction from yellow mustard (Sinapis alba) seed meal with potential application as an additive to calcium-rich drinks
    • Aluko, R. E., M. Reaney, T. McIntosh, F. Ouellet, and F. Katepa-Mupondwa. 2004. Characterization of a calcium-soluble protein fraction from yellow mustard (Sinapis alba) seed meal with potential application as an additive to calcium-rich drinks. J. Agric. Food Chem. 52:6030-6034.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 6030-6034
    • Aluko, R.E.1    Reaney, M.2    McIntosh, T.3    Ouellet, F.4    Katepa-Mupondwa, F.5
  • 8
    • 66149160358 scopus 로고    scopus 로고
    • Comprehensive analysis of the Brassica juncea root proteome in response to cadmium exposure by complementary proteomic approaches
    • Alvarez, S., B. M. Berla, J. Sheffield, R. E. Cahoon, J. M. Jez, and L. M. Hicks. 2009. Comprehensive analysis of the Brassica juncea root proteome in response to cadmium exposure by complementary proteomic approaches. Proteomics 9:2419-2431.
    • (2009) Proteomics , vol.9 , pp. 2419-2431
    • Alvarez, S.1    Berla, B.M.2    Sheffield, J.3    Cahoon, R.E.4    Jez, J.M.5    Hicks, L.M.6
  • 9
    • 34250836448 scopus 로고    scopus 로고
    • Proteomics-based method for the assessment of marine pollution using liquid chromatography coupled with two-dimensional electrophoresis
    • DOI 10.1021/pr060689s
    • Amelina, H., I. Apraiz, W. Sun, and S. Cristobal. 2007. Proteomicsbased method for the assessment of marine pollution using liquid chromatography coupled with two-dimensional electrophoresis. J. Proteome Res. 6:2094-2104. (Pubitemid 46985096)
    • (2007) Journal of Proteome Research , vol.6 , Issue.6 , pp. 2094-2104
    • Amelina, H.1    Apraiz, I.2    Sun, W.3    Cristobal, S.4
  • 11
    • 0023050237 scopus 로고
    • The amino acid sequence of the 2S sulphur-rich protein from seeds of Brazil nut (Bertholletia excelsa H.B.K.)
    • Ampe, C., J. Van Damme, L. A. de Castro, M. J. Sampaio, M. Van Montagu, and J. Vandekerckhove. 1986. The amino acid sequence of the 2S sulphur-rich protein from seeds of Brazil nut (Bertholletia excelsa H.B.K.). Eur. J. Biochem. 159:597-604.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 597-604
    • Ampe, C.1    Van Damme, J.2    De Castro, L.A.3    Sampaio, M.J.4    Van Montagu, M.5    Vandekerckhove, J.6
  • 12
    • 0032051872 scopus 로고    scopus 로고
    • A major protein precursor of zebra mussel (Dreissena polymorpha) byssus: Deduced sequence and significance
    • Anderson, K. E., and J. H. Waite. 1998. A major protein precursor of zebra mussel (Dreissena polymorpha) byssus: deduced sequence and significance. Biol. Bull. 194:150-160. (Pubitemid 28244502)
    • (1998) Biological Bulletin , vol.194 , Issue.2 , pp. 150-160
    • Anderson, K.E.1    Waite, J.H.2
  • 13
    • 0031808711 scopus 로고    scopus 로고
    • The potential of matrix-assisted laser desorption/ionization mass spectrometry in the quality control of water buffalo mozzarella cheese
    • DOI 10.1002/(SICI)1096-9888(199806)33:6<525::AID-JMS655>3.0.CO;2-S
    • Angeletti, R., A. M. Gioacchini, R. Seraglia, R. Piro, and P. Traldi. 1998. The potential of matrix-assisted laser desorption/ionization mass spectrometry in the quality control of water buffalo mozzarella cheese. J. Mass Spectrom. 33:525-531. (Pubitemid 28300263)
    • (1998) Journal of Mass Spectrometry , vol.33 , Issue.6 , pp. 525-531
    • Angeletti, R.1    Gioacchini, A.M.2    Seraglia, R.3    Piro, R.4    Traldi, P.5
  • 14
    • 71549116049 scopus 로고    scopus 로고
    • Peroxisomal proteomics: Biomonitoring in mussels after the Prestige's oil spill
    • Apraiz, I., M. P. Cajaraville, and S. Cristobal. 2009. Peroxisomal proteomics: biomonitoring in mussels after the Prestige's oil spill. Mar. Pollut. Bull. 58:1815-1826.
    • (2009) Mar. Pollut. Bull. , vol.58 , pp. 1815-1826
    • Apraiz, I.1    Cajaraville, M.P.2    Cristobal, S.3
  • 15
    • 33746308468 scopus 로고    scopus 로고
    • Identification of proteomic signatures of exposure to marine pollutants in mussels (Mytilus edulis)
    • DOI 10.1074/mcp.M500333-MCP200
    • Apraiz, I., J. Mi, and S. Cristobal. 2006. Identification of proteomic signatures of exposure to marine pollutants in mussels (Mytilus edulis). Mol. Cell. Proteomics 5:1274-1285. (Pubitemid 44103398)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.7 , pp. 1274-1285
    • Apraiz, I.1    Mi, J.2    Cristobal, S.3
  • 16
    • 0026603940 scopus 로고
    • The use of HPLC protein profiles in fish species identification
    • Armstrong, S. G., D. N. Leach, and S. G. Wyllie. 1992. The use of HPLC protein profiles in fish species identification. Food Chem. 44: 147-155.
    • (1992) Food Chem. , vol.44 , pp. 147-155
    • Armstrong, S.G.1    Leach, D.N.2    Wyllie, S.G.3
  • 17
    • 0010665123 scopus 로고
    • Identification of fish species by high-performance liquid chromatography
    • Ashoor, S. H., and M. J. Knox. 1985. Identification of fish species by high-performance liquid chromatography. J. Chromatogr. 324: 199-202.
    • (1985) J. Chromatogr. , vol.324 , pp. 199-202
    • Ashoor, S.H.1    Knox, M.J.2
  • 18
    • 0023667396 scopus 로고
    • Determination of soy protein, whey protein, and casein in unheated meats by high-performance liquid chromatography
    • Ashoor, S. H., and P. G. Stiles. 1987. Determination of soy protein, whey protein, and casein in unheated meats by high-performance liquid chromatography. J. Chromatogr. 393:321-328.
    • (1987) J. Chromatogr. , vol.393 , pp. 321-328
    • Ashoor, S.H.1    Stiles, P.G.2
  • 19
    • 0023771537 scopus 로고
    • Fast atom bombardment mass spectra of various peptides from sarcoplasmic calcium-binding protein
    • Aubagnac, J. L., A. Salesse, and J. Jauregui-Adell. 1988. Fast atom bombardment mass spectra of various peptides from sarcoplasmic calcium-binding protein. Biomed. Environ. Mass Spectrom. 16:469-472. (Pubitemid 18265834)
    • (1988) Biomedical and Environmental Mass Spectrometry , vol.16 , Issue.1-12 SPEC. ISS. , pp. 469-472
    • Aubagnac, J.L.1    Salesse, A.2    Jauregui-Adell, J.3
  • 20
    • 0029715438 scopus 로고    scopus 로고
    • On hen egg fractionation: Applications of liquid chromatography to the isolation and the purification of hen egg white and egg yolk proteins
    • Awadé, A. C. 1996. On hen egg fractionation: applications of liquid chromatography to the isolation and the purification of hen egg white and egg yolk proteins. Z. Lebensm.-Unters. -Forsch. 202:1-14. (Pubitemid 126798398)
    • (1996) Zeitschrift fur Lebensmittel -Untersuchung und -Forschung , vol.202 , Issue.1 , pp. 1-14
    • Awade, A.C.1
  • 21
    • 0033050814 scopus 로고    scopus 로고
    • Comparison of three liquid chromatographic methods for egg-white protein analysis
    • DOI 10.1016/S0378-4347(98)00538-6, PII S0378434798005386
    • Awadé, A. C., and T. Efstathiou. 1999. Comparison of three liquid chromatographic methods for egg-white protein analysis. J. Chromatogr. B 723:69-74. (Pubitemid 29148110)
    • (1999) Journal of Chromatography B: Biomedical Sciences and Applications , vol.723 , Issue.1-2 , pp. 69-74
    • Awade, A.C.1    Efstathiou, T.2
  • 22
    • 0028023255 scopus 로고
    • Two-step chromatographic procedure for the purification of hen egg white ovomucin, lysozyme, ovotransferrin and ovalbumin and characterization of purified proteins
    • DOI 10.1016/0021-9673(94)80156-8
    • Awadé, A. C., S. Moreau., D. Mollé, G. Brulé, and J. L. Maubois. 1994. Two-step chromatographic procedure for the purification of hen egg white ovomucin, lysozyme, ovotransferrin and ovalbumin and characterization of purified proteins. J. Chromatogr. A 677:279-288. (Pubitemid 24265368)
    • (1994) Journal of Chromatography A , vol.677 , Issue.2 , pp. 279-288
    • Awade, A.C.1    Moreau, S.2    Molle, D.3    Brule, G.4    Maubois, J.-L.5
  • 25
    • 61349150487 scopus 로고    scopus 로고
    • Predictions of peptides' retention times in reversed-phase liquid chromatography as a new supportive tool to improve protein identification in proteomics
    • Baczek, T., and R. Kaliszan. 2009. Predictions of peptides' retention times in reversed-phase liquid chromatography as a new supportive tool to improve protein identification in proteomics. Proteomics 9: 835-847.
    • (2009) Proteomics , vol.9 , pp. 835-847
    • Baczek, T.1    Kaliszan, R.2
  • 26
    • 1642488129 scopus 로고    scopus 로고
    • Nutriproteomics: Identifying the molecular targets of nutritive and non-nutritive components of the diet
    • Barnes, S., and H. Kim. 2004. Nutriproteomics: identifying the molecular targets of nutritive and non-nutritive components of the diet. J. Biochem. Mol. Biol. 37:59-74. (Pubitemid 38402575)
    • (2004) Journal of Biochemistry and Molecular Biology , vol.37 , Issue.1 , pp. 59-74
    • Barnes, S.1    Kim, H.2
  • 27
    • 0023040915 scopus 로고
    • Partial characterization of an allergic glycoprotein from peanut (Arachis hypogaea L.)
    • Barnett, D., and M. E. H. Howden. 1986. Partial characterization of an allergic glycoprotein from peanut (Arachis hypogaea L.). Biochim. Biophys. Acta 882:97-105.
    • (1986) Biochim. Biophys. Acta , vol.882 , pp. 97-105
    • Barnett, D.1    Howden, M.E.H.2
  • 28
    • 37449034027 scopus 로고    scopus 로고
    • Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes
    • Barre, A., C. Sordet, R. Culerrier, F. Rancé, A. Didier, and P. Rougé. 2008. Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes. Mol. Immunol. 45:1231-1240.
    • (2008) Mol. Immunol. , vol.45 , pp. 1231-1240
    • Barre, A.1    Sordet, C.2    Culerrier, R.3    Rancé, F.4    Didier, A.5    Rougé, P.6
  • 29
    • 34547802296 scopus 로고    scopus 로고
    • A proteomic study to identify soya allergens - The human response to transgenic versus non-transgenic soya samples
    • DOI 10.1159/000102611
    • Batista, R., I. Martins, P. Jeno, C. P. Ricardo, and M. M. Oliveira. 2007. A proteomic study to identify soya allergens-the human response to transgenic versus non-transgenic soya samples. Int. Arch. Allergy Immunol. 144:29-38. (Pubitemid 47237666)
    • (2007) International Archives of Allergy and Immunology , vol.144 , Issue.1 , pp. 29-38
    • Batista, R.1    Martins, I.2    Jeno, P.3    Ricardo, C.P.4    Oliveira, M.M.5
  • 31
    • 0028979542 scopus 로고
    • Complete amino acid sequence of the protease inhibitor from buckwheat seeds
    • Belozersky, M. A., Y. E. Dunaevsky, A. X. Musolyamov, and T. A. Egorov. 1995. Complete amino acid sequence of the protease inhibitor from buckwheat seeds. FEBS Lett. 371:264-266.
    • (1995) FEBS Lett. , vol.371 , pp. 264-266
    • Belozersky, M.A.1    Dunaevsky, Y.E.2    Musolyamov, A.X.3    Egorov, T.A.4
  • 32
    • 0034297010 scopus 로고    scopus 로고
    • Complete amino acid sequence of the protease inhibitor BWI-4a from buckwheat seeds
    • Belozersky, M. A., Y. E. Dunaevsky, A. X. Musolyamov, and T. A. Egorov. 2000. Complete amino acid sequence of the protease inhibitor BWI-4a from buckwheat seeds. Biochemistry (Mosc.) 65: 1140-1144.
    • (2000) Biochemistry (Mosc.) , vol.65 , pp. 1140-1144
    • Belozersky, M.A.1    Dunaevsky, Y.E.2    Musolyamov, A.X.3    Egorov, T.A.4
  • 33
    • 0025678423 scopus 로고
    • Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds
    • Belozersky, M. A., Y. E. Dunaevsky, and N. E. Voskoboynikova. 1990. Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds. Biochem. J. 272:677-682.
    • (1990) Biochem. J. , vol.272 , pp. 677-682
    • Belozersky, M.A.1    Dunaevsky, Y.E.2    Voskoboynikova, N.E.3
  • 34
    • 0000975925 scopus 로고
    • Aspartic proteinase from wheat seeds: Isolation, properties and action on gliadin
    • Belozersky, M. A., S. T. Sarbakanova, and Y. E. Dunaevsky. 1988. Aspartic proteinase from wheat seeds: isolation, properties and action on gliadin. Planta 177:321-326.
    • (1988) Planta , vol.177 , pp. 321-326
    • Belozersky, M.A.1    Sarbakanova, S.T.2    Dunaevsky, Y.E.3
  • 35
    • 64549140318 scopus 로고    scopus 로고
    • Offline and online liquid chromatography mass spectrometry in quantitative proteomics
    • Bereszczak, J. Z., and F. L. Brancia. 2009. Offline and online liquid chromatography mass spectrometry in quantitative proteomics. Comb. Chem. High Throughput Screen. 12:185-193.
    • (2009) Comb. Chem. High Throughput Screen. , vol.12 , pp. 185-193
    • Bereszczak, J.Z.1    Brancia, F.L.2
  • 36
    • 0036968792 scopus 로고    scopus 로고
    • Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: Seed storage proteins as common food allergens
    • DOI 10.1067/mai.2002.125487
    • Beyer, K., L. Bardina, G. Grishina, and H. A. Sampson. 2002. Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens. J. Allergy Clin. Immunol. 110:154-159. (Pubitemid 36132742)
    • (2002) Journal of Allergy and Clinical Immunology , vol.110 , Issue.1 , pp. 154-159
    • Beyer, K.1    Bardina, L.2    Grishina, G.3    Sampson, H.A.4
  • 37
    • 0036740044 scopus 로고    scopus 로고
    • Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions
    • Beyer, K., G. Grishina, L. Bardina, A. Grishin, and H. A. Sampson. 2002. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. J. Allergy Clin. Immunol. 110:517-523.
    • (2002) J. Allergy Clin. Immunol. , vol.110 , pp. 517-523
    • Beyer, K.1    Grishina, G.2    Bardina, L.3    Grishin, A.4    Sampson, H.A.5
  • 38
    • 0026692124 scopus 로고
    • Mass spectrometry of peptides and proteins
    • Biemann, K. 1992. Mass spectrometry of peptides and proteins. Annu. Rev. Biochem. 61:977-1010.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 977-1010
    • Biemann, K.1
  • 39
    • 28344444569 scopus 로고    scopus 로고
    • The potential of ecotoxicoproteomics in environmental monitoring: Biomarker profiling in mussel plasma using proteinchip array technology
    • DOI 10.1080/15287390500259277, PII V587266242111
    • Bjørnstad, A., B. K. Larsen, A. Skadsheim, M. B. Jones, and O. K. Andersen. 2006. The potential of ecotoxicoproteomics in environmental monitoring: biomarker profiling in mussel plasma using ProteinChip array technology. J. Toxicol. Environ. Health A 69:77-96. (Pubitemid 41715159)
    • (2006) Journal of Toxicology and Environmental Health - Part A , vol.69 , Issue.1-2 , pp. 77-96
    • Bjornstad, A.1    Larsen, B.K.2    Skadsheim, A.3    Jones, M.B.4    Andersen, O.K.5
  • 40
    • 77949599395 scopus 로고    scopus 로고
    • Data-independent liquid chromatography/mass spectrometry (LC/MS(E)) detection and quantification of the secreted Apium graveolens pathogen defense protein mannitol dehydrogenase
    • Blackburn, K., F. Y. Cheng, J. D. Williamson, and M. B. Goshe. 2010. Data-independent liquid chromatography/mass spectrometry (LC/MS(E)) detection and quantification of the secreted Apium graveolens pathogen defense protein mannitol dehydrogenase. Rapid Commun. Mass Spectrom. 24:1009-1016.
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 1009-1016
    • Blackburn, K.1    Cheng, F.Y.2    Williamson, J.D.3    Goshe, M.B.4
  • 41
    • 0345643467 scopus 로고    scopus 로고
    • Identification of wheat varieties using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry and an artificial neural network
    • DOI 10.1002/(SICI)1097-0231(19990730)13:14<1535::AID-RCM686>3.0. CO;2-U
    • Bloch, H. A., C. Kesmir, M. Petersen, S. Jacobsen, and I. I. Søndergaard. 1999. Identification of wheat varieties using matrixassisted laser desorption/ionisation time-of-flight mass spectrometry and an artificial neural network. Rapid Commun. Mass Spectrom. 13:1535-1539. (Pubitemid 29345309)
    • (1999) Rapid Communications in Mass Spectrometry , vol.13 , Issue.14 , pp. 1535-1539
    • Bloch, H.A.1    Kesmir, C.2    Petersen, M.3    Jacobsen, S.4    Sondergaard, I.5
  • 43
    • 0037106398 scopus 로고    scopus 로고
    • Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry
    • Bondarenko, P. V., D. Chelius, and T. A. Shaler. 2002. Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry. Anal. Chem. 74:4741-4749.
    • (2002) Anal. Chem. , vol.74 , pp. 4741-4749
    • Bondarenko, P.V.1    Chelius, D.2    Shaler, T.A.3
  • 44
    • 44749087402 scopus 로고    scopus 로고
    • Validation of a new reversed-phase high-performance liquid chromatography method for separation and quantification of bovine milk protein genetic variants
    • Bonfatti, V., L. Grigoletto, A. Cecchinato, L. Galloa, and P. Carnier. 2008. Validation of a new reversed-phase high-performance liquid chromatography method for separation and quantification of bovine milk protein genetic variants. J. Chromatogr. A 1195:101-106.
    • (2008) J. Chromatogr. A , vol.1195 , pp. 101-106
    • Bonfatti, V.1    Grigoletto, L.2    Cecchinato, A.3    Galloa, L.4    Carnier, P.5
  • 45
    • 57749201362 scopus 로고    scopus 로고
    • Quantification of bovine casein fractions by direct chromatographic analysis of milk. Approaching the application to a real production context
    • Bonizzi, I., J. N. Buffoni, and M. Feligini. 2009. Quantification of bovine casein fractions by direct chromatographic analysis of milk. Approaching the application to a real production context. J. Chromatogr. A 1216:165-168.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 165-168
    • Bonizzi, I.1    Buffoni, J.N.2    Feligini, M.3
  • 46
    • 17444392125 scopus 로고    scopus 로고
    • Application of isotope coded affinity tag (ICAT) analysis for the identification of differentially expressed proteins following infection of Atlantic salmon (Salmo salar) with infectious hematopoietic necrosis virus (IHNV) or Renibacterium salmoninarum (BKD)
    • DOI 10.1021/pr049840t
    • Booy, A. T., J. D. Haddow, L. B. Ohlund, D. B. Hardie, and R. W. Olafson. 2005. Application of isotope coded affinity tag (ICAT) analysis for the identification of differentially expressed proteins following infection of Atlantic salmon (Salmo salar) with infectious hematopoietic necrosis virus (IHNV) or Renibacterium salmoninarum (BKD). J. Proteome Res. 4:325-334. (Pubitemid 40548136)
    • (2005) Journal of Proteome Research , vol.4 , Issue.2 , pp. 325-334
    • Booy, A.T.1    Haddow, J.D.2    Ohlund, L.B.3    Hardie, D.B.4    Olafson, R.W.5
  • 47
    • 0034510175 scopus 로고    scopus 로고
    • Characterization of a goat whey peptic hydrolysate produced by an ultrafiltration membrane enzymic reactor
    • DOI 10.1017/S0022029900004416
    • Bordenave, B. S., F. Sannier, G. Ricart, and J. M. Piot. 2000. Characterization of a goat whey peptic hydrolysate produced by an ultrafiltration membrane enzymic reactor. J. Dairy Res. 67:551-559. (Pubitemid 32122070)
    • (2000) Journal of Dairy Research , vol.67 , Issue.4 , pp. 551-559
    • Bordenave, S.1    Sannier, F.2    Ricart, G.3    Piot, J.-M.4
  • 48
    • 0035979766 scopus 로고    scopus 로고
    • Identification and quantification of major bovine milk proteins by liquid chromatography
    • DOI 10.1016/S0021-9673(01)01097-4, PII S0021967301010974
    • Bordin, G., F. Cordeiro Raposo, B. de la Calle, and A. R. Rodriguez. 2001. Identification and quantification of major bovine milk proteins by liquid chromatography. J. Chromatogr. A 928:63-76. (Pubitemid 32786874)
    • (2001) Journal of Chromatography A , vol.928 , Issue.1 , pp. 63-76
    • Bordin, G.1    Cordeiro Raposo, F.2    De La Calle, B.3    Rodriguez, A.R.4
  • 49
    • 0037991120 scopus 로고    scopus 로고
    • s2-, β- and κ-caseins by hydrophobic interaction chromatography in cows', ewes' and goats' milk, milk mixtures and cheeses
    • DOI 10.1016/S0021-9673(03)00483-7
    • Bramanti, E., C. Sortino, M. Onor, F. Beni, and G. Raspi. 2003. Separation and determination of denatured alpha(s1)-, alpha(s2)-, beta-and kappa-caseins by hydrophobic interaction chromatography in cows', ewes' and goats' milk, milk mixtures and cheeses. J. Chromatogr. A 994:59-74. (Pubitemid 36549094)
    • (2003) Journal of Chromatography A , vol.994 , Issue.1-2 , pp. 59-74
    • Bramanti, E.1    Sortino, C.2    Onor, M.3    Beni, F.4    Raspi, G.5
  • 50
    • 60349105480 scopus 로고    scopus 로고
    • A label-free internal standard method for the differential analysis of bioactive lupin proteins using nano HPLC-chip coupled with ion trap mass spectrometry
    • Brambilla, F., D. Resta, I. Isak, M. Zanotti, and A. Arnoldi. 2009. A label-free internal standard method for the differential analysis of bioactive lupin proteins using nano HPLC-chip coupled with ion trap mass spectrometry. Proteomics 9:272-286.
    • (2009) Proteomics , vol.9 , pp. 272-286
    • Brambilla, F.1    Resta, D.2    Isak, I.3    Zanotti, M.4    Arnoldi, A.5
  • 51
    • 0036211212 scopus 로고    scopus 로고
    • Contribution of Lactococcus lactis cell envelope proteinase specificity to peptide accumulation and bitterness in reduced-fat cheddar cheese
    • DOI 10.1128/AEM.68.4.1778-1785.2002
    • Broadbent, J. R., M. Barnes, C. Brennand, M. Strickland, K. Houck, M. E. Johnson, and J. L. Steele. 2002. Contribution of Lactococcus lactis cell envelope proteinase specificity to peptide accumulation and bitterness in reduced-fat Cheddar cheese. Appl. Environ. Microbiol. 68:1778-1785. (Pubitemid 34279985)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.4 , pp. 1778-1785
    • Broadbent, J.R.1    Barnes, M.2    Brennand, C.3    Strickland, M.4    Houck, K.5    Johnson, M.E.6    Steele, J.L.7
  • 53
    • 0141483499 scopus 로고    scopus 로고
    • Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients
    • Bublin, M., C. Radauer, I. B. Wilson, D. Kraft, O. Scheiner, H. Breiteneder, and K. Hoffmann-Sommergruber. 2003. Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients. FASEB J. 17: 1697-1699.
    • (2003) FASEB J. , vol.17 , pp. 1697-1699
    • Bublin, M.1    Radauer, C.2    Wilson, I.B.3    Kraft, D.4    Scheiner, O.5    Breiteneder, H.6    Hoffmann-Sommergruber, K.7
  • 54
    • 0037859626 scopus 로고
    • Soybean cultivar identification using high performance liquid chromatography of seed proteins
    • Buehler, R. E., M. B. McDonald, Jr., T. T. Van Toai, and S. K. St. Martin. 1989. Soybean cultivar identification using high performance liquid chromatography of seed proteins. Crop Sci. 29:32-37.
    • (1989) Crop Sci. , vol.29 , pp. 32-37
    • Buehler, R.E.1    McDonald Jr., M.B.2    Van Toai, T.T.3    Martin, S.K.4
  • 55
    • 0344467332 scopus 로고
    • The optimisation of elution and extraction conditions for the separation of soybean seed proteins using RP-HPLC
    • Buehler, R. E., T. T. Van Toai, and M. B. McDonald, Jr. 1989. The optimisation of elution and extraction conditions for the separation of soybean seed proteins using RP-HPLC. Seed Sci. Technol. 17: 193-204.
    • (1989) Seed Sci. Technol. , vol.17 , pp. 193-204
    • Buehler, R.E.1    Van Toai, T.T.2    McDonald Jr., M.B.3
  • 56
    • 0013425296 scopus 로고
    • Reversed-phase highperformance liquid chromatography of durum wheat gliadins: Relationships to durum wheat quality
    • Burnouf, T., and J. A. Bietz. 1984. Reversed-phase highperformance liquid chromatography of durum wheat gliadins: relationships to durum wheat quality. J. Cereal Sci. 2:3-14.
    • (1984) J. Cereal Sci. , vol.2 , pp. 3-14
    • Burnouf, T.1    Bietz, J.A.2
  • 57
    • 0000138954 scopus 로고    scopus 로고
    • Evidence of multiple glycosylation of bovine β-lactoglobulin by electrospray ionisation mass spectrometry
    • Burr, R., C. H. Moore, and J. P. Hill. 1996. Evidence of multiple glycosylation of bovine β-lactoglobulin by electrospray ionization mass spectrometry. Milchwissenschaft 51:488-492. (Pubitemid 126346017)
    • (1996) Milchwissenschaft , vol.51 , Issue.9 , pp. 488-492
    • Burr, R.1    Moore, C.H.2    Hill, J.P.3
  • 58
    • 0034641671 scopus 로고    scopus 로고
    • Cross-linking in adhesive quinoproteins: Studies with model decapeptides
    • Burzio, L. A., and J. H. Waite. 2000. Cross-linking in adhesive quinoproteins: studies with model decapeptides. Biochemistry 39: 11147-11153.
    • (2000) Biochemistry , vol.39 , pp. 11147-11153
    • Burzio, L.A.1    Waite, J.H.2
  • 59
    • 0030968034 scopus 로고    scopus 로고
    • Sample preparation optimization far the analysis of gliadins in food by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • DOI 10.1002/(SICI)1096-9888(199704)32:4<444::AID-JMS500>3.0.CO;2-U
    • Camafeita, E., P. Alfonso, B. Acevedo, and E. Méndez. 1997. Sample preparation optimization for the analysis of gliadins in food by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 32:444-449. (Pubitemid 27171163)
    • (1997) Journal of Mass Spectrometry , vol.32 , Issue.4 , pp. 444-449
    • Camafeita, E.1    Alfonso, P.2    Acevedo, B.3    Mendez, E.4
  • 60
    • 0030758950 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometric micro-analysis: The first non-immunological alternative attempt to quantify gluten gliadins in food samples
    • DOI 10.1002/(SICI)1096-9888(199709)32:9<940::AID-JMS550>3.0.CO;2-2
    • Camafeita, E., P. Alfonso, T. Mothes, and E. Méndez. 1997. Matrixassisted laser desorption/ionization time-of-flight mass spectrometric micro-analysis: the first non-immunological alternative attempt to quantify gluten gliadins in food samples. J. Mass Spectrom. 32: 940-947. (Pubitemid 27380200)
    • (1997) Journal of Mass Spectrometry , vol.32 , Issue.9 , pp. 940-947
    • Camafeita, E.1    Alfonso, P.2    Mothes, T.3    Mendez, E.4
  • 61
    • 0031795336 scopus 로고    scopus 로고
    • Screening of gluten avenins in foods by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • DOI 10.1002/(SICI)1096-9888(1998100)33:10<1023::AID-JMS723>3.0. CO;2-V
    • Camafeita, E., and E. Méndez. 1998. Screening of gluten avenins in foods by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 33:1023-1028. (Pubitemid 28499672)
    • (1998) Journal of Mass Spectrometry , vol.33 , Issue.10 , pp. 1023-1028
    • Camafeita, E.1    Mendez, E.2
  • 62
    • 0032500652 scopus 로고    scopus 로고
    • Selective identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of different types of gluten in foods made with cereal mixtures
    • DOI 10.1016/S0021-9673(98)00621-9, PII S0021967398006219
    • Camafeita, E., J. Solís, P. Alfonso, J. A. López, L. Sorell, and E. Méndez. 1998. Selective identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of different types of gluten in foods made with cereal mixtures. J. Chromatogr. A 823:299-306. (Pubitemid 28461832)
    • (1998) Journal of Chromatography A , vol.823 , Issue.1-2 , pp. 299-306
    • Camafeita, E.1    Solis, J.2    Alfonso, P.3    Lopez, J.A.4    Sorell, L.5    Mendez, E.6
  • 63
    • 0037073082 scopus 로고    scopus 로고
    • Recent advances in the application of mass spectrometry in food-related analysis
    • DOI 10.1016/S0021-9673(02)00903-2, PII S0021967302009032
    • Careri, M., F. Bianchi, and C. Corradini. 2002. Recent advances in the application of mass spectrometry in food-related analysis. J. Chromatogr. A 970:3-64. (Pubitemid 35286569)
    • (2002) Journal of Chromatography A , vol.970 , Issue.1-2 , pp. 3-64
    • Careri, M.1    Bianchi, F.2    Corradini, C.3
  • 64
    • 36849082932 scopus 로고    scopus 로고
    • Use of specific peptide biomarkers for quantitative confirmation of hidden allergenic peanut proteins Ara h 2 and Ara h 3/4 for food control by liquid chromatography-tandem mass spectrometry
    • DOI 10.1007/s00216-007-1595-2, Pesticides in Food
    • Careri, M., A. Costa, L. Elviri, J. B. Lagos, A. Mangia, M. Terenghi, A. Cereti, and L. P. Garoffo. 2007. Use of specific peptide biomarkers for quantitative confirmation of hidden allergenic peanut proteins Ara h 2 and Ara h 3/4 for food control by liquid chromatography-tandem mass spectrometry. Anal. Bioanal. Chem. 389:1901-1907. (Pubitemid 350231593)
    • (2007) Analytical and Bioanalytical Chemistry , vol.389 , Issue.6 , pp. 1901-1907
    • Careri, M.1    Costa, A.2    Elviri, L.3    Lagos, J.-B.4    Mangia, A.5    Terenghi, M.6    Cereti, A.7    Garoffo, L.P.8
  • 65
    • 51549117850 scopus 로고    scopus 로고
    • Selective and rapid immunomagnetic bead-based sample treatment for the liquid chromatography-electrospray iontrap mass spectrometry detection of Ara h3/4 peanut protein in foods
    • Careri, M., L. Elviri, J. B. Lagos, A. Mangia, F. Speroni, and M. Terenghi. 2008. Selective and rapid immunomagnetic bead-based sample treatment for the liquid chromatography-electrospray iontrap mass spectrometry detection of Ara h3/4 peanut protein in foods. J. Chromatogr. A 1206:89-94.
    • (2008) J. Chromatogr. A , vol.1206 , pp. 89-94
    • Careri, M.1    Elviri, L.2    Lagos, J.B.3    Mangia, A.4    Speroni, F.5    Terenghi, M.6
  • 66
    • 41149177388 scopus 로고    scopus 로고
    • Determination of peanut allergens in cereal-chocolate-based snacks: Metal-tag inductively coupled plasma mass spectrometry immunoassay versus liquid chromatography/electrospray ionization tandem mass spectrometry
    • DOI 10.1002/rcm.3427
    • Careri, M., L. Elviri, M. Maffini, A. Mangia, C. Mucchino, and M. Terenghi. 2008. Determination of peanut allergens in cerealchocolate-based snacks: metal-tag inductively coupled plasma mass spectrometry immunoassay versus liquid chromatography/electrospray ionization tandem mass spectrometry. Rapid Commun. Mass Spectrom. 22:807-811. (Pubitemid 351442554)
    • (2008) Rapid Communications in Mass Spectrometry , vol.22 , Issue.6 , pp. 807-811
    • Careri, M.1    Elviri, L.2    Maffini, M.3    Mangia, A.4    Mucchino, C.5    Terenghi, M.6
  • 67
    • 0038777519 scopus 로고    scopus 로고
    • Analysis of food proteins and peptides by chromatography and mass spectrometry
    • DOI 10.1016/S0021-9673(03)00237-1
    • Careri, M., and A. Mangia. 2003. Analysis of food proteins and peptides by chromatography and mass spectrometry. J. Chromatogr. A 1000:609-635. (Pubitemid 36638477)
    • (2003) Journal of Chromatography A , vol.1000 , Issue.1-2 , pp. 609-635
    • Careri, M.1    Mangia, A.2
  • 68
    • 33749590936 scopus 로고    scopus 로고
    • Identification of commercial hake and grenadier species by proteomic analysis of the parvalbumin fraction
    • DOI 10.1002/pmic.200500899
    • Carrera, M., B. Cañ as, C. Piñ eiro, J. Vázquez, and J. M. Gallardo. 2006. Identification of commercial hake and grenadier species by proteomic analysis of the parvalbumin fraction. Proteomics 6:5278-5287. (Pubitemid 44547166)
    • (2006) Proteomics , vol.6 , Issue.19 , pp. 5278-5287
    • Carrera, M.1    Canas, B.2    Pineiro, C.3    Vazquez, J.4    Gallardo, J.M.5
  • 69
    • 34548153081 scopus 로고    scopus 로고
    • De novo mass spectrometry sequencing and characterization of species-specific peptides from nucleoside diphosphate kinase B for the classification of commercial fish species belonging to the family merlucciidae
    • DOI 10.1021/pr0701963
    • Carrera, M., B. Cañas, C. Piñeiro, J. Vázquez, and J. M. Gallardo. 2007. De novo mass spectrometry sequencing and characterization of species-specific peptides from nucleoside diphosphate kinase B for the classification of commercial fish species belonging to the family Merlucciidae. J. Proteome Res. 6:3070-3080. (Pubitemid 47310192)
    • (2007) Journal of Proteome Research , vol.6 , Issue.8 , pp. 3070-3080
    • Carrera, M.1    Canas, B.2    Pineiro, C.3    Vazquez, J.4    Gallardo, J.M.5
  • 70
    • 33745949907 scopus 로고    scopus 로고
    • Determination of soybean proteins in soybean-wheat and soybean-rice commercial products by perfusion reversed-phase high-performance liquid chromatography
    • DOI 10.1016/j.foodchem.2005.10.060, PII S030881460500960X
    • Castro-Rubio, A., F. Castro-Rubio, M. C. García, and M. L. Marina. 2007. Determination of soybean proteins in soybean-wheat and soybean-rice commercial products by perfusion reversed-phase high-performance liquid chromatography. Food Chem. 100:948-955. (Pubitemid 44062172)
    • (2007) Food Chemistry , vol.100 , Issue.3 , pp. 948-955
    • Castro-Rubio, A.1    Castro-Rubio, F.2    Garcia, M.C.3    Marina, M.L.4
  • 71
    • 31044451401 scopus 로고    scopus 로고
    • Rapid separation of soybean and cereal (wheat, corn, and rice) proteins in complex mixtures: Application to the selective determination of the soybean protein content in commercial cereal-based products
    • DOI 10.1016/j.aca.2005.10.076, PII S0003267005018520
    • Castro-Rubio, A., M. C. García, and M. L. Marina. 2006. Rapid separation of soybean and cereal (wheat, corn, and rice) proteins in complex mixtures: application to the selective determination of the soybean protein content in commercial cereal-based products. Anal. Chim. Acta 558:28-34. (Pubitemid 43120485)
    • (2006) Analytica Chimica Acta , vol.558 , Issue.1-2 , pp. 28-34
    • Castro-Rubio, A.1    Garcia, M.C.2    Marina, M.L.3
  • 72
    • 0030468685 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry in milk science
    • DOI 10.1002/(SICI)1097-0231(199610)10:13<1629::AID-RCM655>3.0.CO;2- B
    • Catinella, S., P. Traldi, C. Pinelli, E. Dallaturca, and R. Marsilio. 1996. Matrix-assisted laser desorption/ionization mass spectrometry in milk science. Rapid Commun. Mass Spectrom. 10:1629-1637. (Pubitemid 27040295)
    • (1996) Rapid Communications in Mass Spectrometry , vol.10 , Issue.13 , pp. 1629-1637
    • Catinella, S.1    Traldi, P.2    Pinelli, C.3    Dallaturca, E.4    Marsilio, R.5
  • 73
    • 0001208610 scopus 로고
    • Sample preparation for selective and sensitive detection of soya proteins in dairy products with chromatographic and electrophoretic techniques
    • Cattaneo, T. M. P., A. Feroldi, P. M. Toppino, and C. Olieman. 1994. Sample preparation for selective and sensitive detection of soya proteins in dairy products with chromatographic and electrophoretic techniques. Neth. Milk Dairy J. 48:225-234.
    • (1994) Neth. Milk Dairy J. , vol.48 , pp. 225-234
    • Cattaneo, T.M.P.1    Feroldi, A.2    Toppino, P.M.3    Olieman, C.4
  • 74
    • 84985108885 scopus 로고
    • Protein composition of seeds of Lupinus albus
    • Cerletti, P., A. Fumagalli, and D. Venturin. 1978. Protein composition of seeds of Lupinus albus. J. Food Sci. 43:1409-1411.
    • (1978) J. Food Sci. , vol.43 , pp. 1409-1411
    • Cerletti, P.1    Fumagalli, A.2    Venturin, D.3
  • 75
    • 34250652972 scopus 로고    scopus 로고
    • Proteomics-based approach to detect and identify major allergens in processed peanuts by capillary LC-Q-TOF (MS/MS)
    • DOI 10.1021/jf063630e
    • Chassaigne, H., J. V. Nørgaard, and A. J. van Hengel. 2007. Proteomics-based approach to detect and identify major allergens in processed peanuts by capillary LC-Q-TOF (MS/MS). J. Agric. Food Chem. 55:4461-4473. (Pubitemid 46932643)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.11 , pp. 4461-4473
    • Chassaigne, H.1    Norgaard, J.V.2    Van Hengel, A.J.3
  • 76
    • 63349087317 scopus 로고    scopus 로고
    • Resolution and identification of major peanut allergens using a combination of fluorescence two-dimensional differential gel electrophoresis, Western blotting and Q-TOF mass spectrometry
    • Chassaigne, H., V. Trégoat, J. V. Nørgaard, S. J. Maleki, and A. J. van Hengel. 2009. Resolution and identification of major peanut allergens using a combination of fluorescence two-dimensional differential gel electrophoresis, Western blotting and Q-TOF mass spectrometry. J. Proteomics 72:511-526.
    • (2009) J. Proteomics , vol.72 , pp. 511-526
    • Chassaigne, H.1    Trégoat, V.2    Nørgaard, J.V.3    Maleki, S.J.4    Van Hengel, A.J.5
  • 77
    • 33644506769 scopus 로고    scopus 로고
    • Study of thermal aggregation of globulin from common buckwheat (Fagopyrum esculentum Moench) by size-exclusion chromatography and laser light scattering
    • Choi, S. M., and C.-Y. Ma. 2006. Study of thermal aggregation of globulin from common buckwheat (Fagopyrum esculentum Moench) by size-exclusion chromatography and laser light scattering. J. Agric. Food Chem. 54:554-561.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 554-561
    • Choi, S.M.1    Ma, C.-Y.2
  • 78
    • 33748697399 scopus 로고    scopus 로고
    • Extraction, purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds
    • DOI 10.1016/j.foodres.2006.06.004, PII S0963996906000937
    • Choi, S. M., and C.-Y. Ma. 2006. Extraction, purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds. Food Res. Int. 39:974-981. (Pubitemid 44397551)
    • (2006) Food Research International , vol.39 , Issue.9 , pp. 974-981
    • Choi, S.-M.1    Ma, C.-Y.2
  • 79
    • 0000352284 scopus 로고
    • Size exclusion chromatography of soybean proteins and isoflavones
    • Cole, K. D., and S. L. Cousin, Jr. 1994. Size exclusion chromatography of soybean proteins and isoflavones. J. Agric. Food Chem. 42:2713-2720.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 2713-2720
    • Cole, K.D.1    Cousin Jr., S.L.2
  • 80
    • 67649710064 scopus 로고    scopus 로고
    • Untargeted LC-Q-TOF mass spectrometry method for the detection of adulterations in skimmedmilk powder
    • Cordewener, J. H., D. M. Luykx, R. Frankhuizen, M. G. Bremer, H. Hooijerink, and A. H. America. 2009. Untargeted LC-Q-TOF mass spectrometry method for the detection of adulterations in skimmedmilk powder. J. Sep. Sci. 32:1216-1223.
    • (2009) J. Sep. Sci. , vol.32 , pp. 1216-1223
    • Cordewener, J.H.1    Luykx, D.M.2    Frankhuizen, R.3    Bremer, M.G.4    Hooijerink, H.5    America, A.H.6
  • 81
    • 0000135160 scopus 로고
    • Characterisation of gluten subfractions by SE-HPLC and dynamic rheological analysis in shear
    • Cornec, M., Y. Popineau, and J. Lefebvre. 1994. Characterisation of gluten subfractions by SE-HPLC and dynamic rheological analysis in shear. J. Cereal Sci. 19:131-139.
    • (1994) J. Cereal Sci. , vol.19 , pp. 131-139
    • Cornec, M.1    Popineau, Y.2    Lefebvre, J.3
  • 82
    • 0034999623 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometric peptide mapping of high molecular weight glutenin subunits 1Bx7 and 1Dy10 in Cheyenne cultivar
    • DOI 10.1002/rcm.299
    • Cozzolino, R., S. Di Giorgi, S. Fisichella, D. Garozzo, D. Lafiandra., and A. Palermo. 2001. Matrix-assisted laser desorption/ ionization mass spectrometric peptide mapping of high molecular weight glutenin subunits 1Bx7 and 1Dy10 in Cheyenne cultivar. Rapid Commun. Mass Spectrom. 15:778-787. (Pubitemid 32479840)
    • (2001) Rapid Communications in Mass Spectrometry , vol.15 , Issue.10 , pp. 778-787
    • Cozzolino, R.1    Di Giorgi, S.2    Fisichella, S.3    Garozzo, D.4    Lafiandra, D.5    Palermo, A.6
  • 83
    • 0034913170 scopus 로고    scopus 로고
    • Proteomics of gluten: Mapping of subunit 1 Ax2*in Cheyenne cultivar by matrix-assisted laser desorption/ionization
    • DOI 10.1002/rcm.354
    • Cozzolino, R., S. Di Giorgi, S. Fisichella, D. Garozzo, D. Lafiandra, and A. Palermo. 2001. Proteomics of gluten: mapping of subunit 1 Ax2* in Cheyenne cultivar by matrix-assisted laser desorption/ ionization. Rapid Commun. Mass Spectrom. 15:1129-1135. (Pubitemid 32674832)
    • (2001) Rapid Communications in Mass Spectrometry , vol.15 , Issue.14 , pp. 1129-1135
    • Cozzolino, R.1    Di Giorgi, S.2    Fisichella, S.3    Garozzo, D.4    Lafiandra, D.5    Palermo, A.6
  • 84
    • 33644660121 scopus 로고    scopus 로고
    • Capillary liquid chromatography/atmospheric-pressure matrix-assisted laser desorption/ionisation ion trap mass spectrometry: A comparison with liquid chromatography/matrix-assisted laser desorption/ionisation time-of-flight and liquid chromatography/electrospray ionisation quadrupole time-of-flight for the identification of tryptic peptides
    • DOI 10.1002/rcm.2376
    • Creaser, C. S., P. S. Green, P. M. Kilby, and L. Ratcliffe. 2006. Capillary liquid chromatography/atmospheric-pressure matrixassisted laser desorption/ionisation ion trap mass spectrometry: a comparison with liquid chromatography/matrix-assisted laser desorption/ionisation time-of-flight and liquid chromatography/ electrospray ionisation quadrupole time-of-flight for the identification of tryptic peptides. Rapid Commun. Mass Spectrom. 20:829-836. (Pubitemid 43326690)
    • (2006) Rapid Communications in Mass Spectrometry , vol.20 , Issue.5 , pp. 829-836
    • Creaser, C.S.1    Green, P.S.2    Kilby, P.M.3    Ratcliffe, L.4
  • 85
    • 3242713358 scopus 로고    scopus 로고
    • Mass spectrometry in the characterisation of cereal seed proteins
    • DOI 10.1255/ejms.609
    • Cunsolo, V., S. Foti, and R. Saletti. 2004. Mass spectrometry in the characterization of cereal seed proteins. Eur. J. Mass Spectrom. 10: 359-370. (Pubitemid 38887058)
    • (2004) European Journal of Mass Spectrometry , vol.10 , Issue.3 SPEC. ISS. , pp. 359-370
    • Cunsolo, V.1    Foti, S.2    Saletti, R.3
  • 86
    • 0036388226 scopus 로고    scopus 로고
    • Investigation and correction of the gene-derived sequence of glutenin subunit 1Dx2 by matrix-assisted laser desorption/ionisation mass spectrometry
    • Cunsolo, V., S. Foti, R. Saletti, S. Gilbert, A. S. Tatham, and P. R. Shewry. 2002. Investigation and correction of the gene-derived sequence of glutenin subunit 1Dx2 by matrix-assisted laser desorption/ionisation mass spectrometry. Rapid Commun. Mass Spectrom. 16:1911-1918.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 1911-1918
    • Cunsolo, V.1    Foti, S.2    Saletti, R.3    Gilbert, S.4    Tatham, A.S.5    Shewry, P.R.6
  • 87
    • 0037288471 scopus 로고    scopus 로고
    • Structural studies of glutenin subunits 1Dy10 and 1Dy12 by matrix-assisted laser desorption/ionisation mass spectrometry and high-performance liquid chromatography/electrospray ionisation mass spectrometry
    • DOI 10.1002/rcm.938
    • Cunsolo, V., S. Foti, R. Saletti, S. Gilbert, A. S. Tatham, and P. R. Shewry. 2003. Structural studies of glutenin subunits 1Dy10 and 1Dy12 by matrix-assisted laser desorption/ionisation mass spectrometry and high-performance liquid chromatography/electrospray ionisation mass spectrometry. Rapid Commun. Mass Spectrom. 17: 442-454. (Pubitemid 36267980)
    • (2003) Rapid Communications in Mass Spectrometry , vol.17 , Issue.5 , pp. 442-454
    • Cunsolo, V.1    Foti, S.2    Saletti, R.3    Gilbert, S.4    Tatham, A.S.5    Shewry, P.R.6
  • 88
    • 1142275173 scopus 로고    scopus 로고
    • Structural studies of the allelic wheat glutenin subunits 1BX7 and 1Bx20 by matrix-assisted laser desorption/ionization mass spectrometry and high-performance liquid chromatography/electrospray ionization mass spectrometry
    • DOI 10.1002/jms.558
    • Cunsolo, V., S. Foti, R. Saletti, S. Gilbert, A. S. Tatham, and P. R. Shewry. 2004. Structural studies of the allelic wheat glutenin subunits 1Bx7 and 1Bx20 by matrix-assisted laser desorption/ ionization mass spectrometry and high-performance liquid chromatography/ electrospray ionization mass spectrometry. J. Mass Spectrom. 39:66-78. (Pubitemid 38208533)
    • (2004) Journal of Mass Spectrometry , vol.39 , Issue.1 , pp. 66-78
    • Cunsolo, V.1    Foti, S.2    Saletti, R.3    Gilbert, S.4    Tatham, A.S.5    Shewry, P.R.6
  • 89
    • 34547236610 scopus 로고    scopus 로고
    • Absolute quantitation of β-lactoglobulin by protein liquid chromatography-mass spectrometry and its application to different milk products
    • DOI 10.1021/ac062367d
    • Czerwenka, C., I. Maier, N. Potocnik, F. Pittner, and W. Lindner. 2007. Absolute quantitation of beta-lactoglobulin by protein liquid chromatography-mass spectrometry and its application to different milk products. Anal. Chem. 79:5165-5172. (Pubitemid 47121026)
    • (2007) Analytical Chemistry , vol.79 , Issue.14 , pp. 5165-5172
    • Czerwenka, C.1    Maier, I.2    Potocnik, N.3    Pittner, F.4    Lindner, W.5
  • 90
    • 77249107516 scopus 로고    scopus 로고
    • The egg white and yolk interactomes as gleaned from extensive proteomic data
    • D'Alessandro, A., P. G. Righetti, E. Fasoli, and L. Zolla. 2010. The egg white and yolk interactomes as gleaned from extensive proteomic data. J. Proteomics 73:1028-1042.
    • (2010) J. Proteomics , vol.73 , pp. 1028-1042
    • D'Alessandro, A.1    Righetti, P.G.2    Fasoli, E.3    Zolla, L.4
  • 92
    • 0026940088 scopus 로고
    • Rapid analysis of whey proteins from different animal species by reversed-phase high-performance liquid chromatography
    • De Frutos, M., A. Cifuentes, L. Amigo, M. Ramos, and J. C. Diez-Masa. 1992. Rapid analysis of whey proteins from different animal species by reversed-phase high-performance liquid chromatography. Z. Lebensm.-Unters. -Forsch. 195:326-331.
    • (1992) Z. Lebensm.-Unters.-Forsch. , vol.195 , pp. 326-331
    • De Frutos, M.1    Cifuentes, A.2    Amigo, L.3    Ramos, M.4    Diez-Masa, J.C.5
  • 93
    • 0031693497 scopus 로고    scopus 로고
    • Multiple peaks in HPLC of proteins: Bovine serum albumin eluted in a reversed-phase system
    • DOI 10.1002/(SICI)1521-4168(19980101)21:1<18::AID-JHRC18>3.0.CO;2-5
    • De Frutos, M., A. Cifuentes, J. C. Díez-Masa, E. Camafeita, and E. Méndez. 1998. Multiple peaks in HPLC of proteins: bovine serum albumin eluted in a reversed-phase system. J. High Resol. Chromatogr. 21:18-24. (Pubitemid 28423772)
    • (1998) HRC Journal of High Resolution Chromatography , vol.21 , Issue.1 , pp. 18-24
    • De Frutos, M.1    Cifuentes, A.2    Diez-Masa, J.C.3    Camafeita, E.4    Mendez, E.5
  • 94
    • 0342310189 scopus 로고
    • Potential use of electrospray ionization mass spectrometry for the detection of irradiated egg white
    • Deighton, N., S. M. Glidewell, and B. A. Goodman. 1995. Potential use of electrospray ionization mass spectrometry for the detection of irradiated egg white. Food Sci. Technol. Today 9:144-145.
    • (1995) Food Sci. Technol. Today , vol.9 , pp. 144-145
    • Deighton, N.1    Glidewell, S.M.2    Goodman, B.A.3
  • 95
    • 33845732197 scopus 로고    scopus 로고
    • ICP-MS-assisted nanoHPLC-electrospray Q/time-of-flight MS/MS selenopeptide mapping in Brazil nuts
    • DOI 10.1039/b608041c
    • Dernovics, M., P. Giusti, and R. Lobinski. 2006. ICP-MS-assisted nanoHPLC-electrospray Q/time-of-flight MS/MS selenopeptide mapping in Brazil nuts. J. Anal. At. Spectrom. 22:41-50. (Pubitemid 44975075)
    • (2007) Journal of Analytical Atomic Spectrometry , vol.22 , Issue.1 , pp. 41-50
    • Dernovics, M.1    Giusti, P.2    Lobinski, R.3
  • 96
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon, B., and R. Aebersold. 2006. Mass spectrometry and protein analysis. Science 312:212-217.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 97
    • 68849130823 scopus 로고    scopus 로고
    • Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals
    • Dooper, M. M., C. Plassen, L. Holden, H. Lindvik, and C. K. Fæste. 2009. Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals. J. Investig. Allergol. Clin. Immunol. 19:283-291.
    • (2009) J. Investig. Allergol. Clin. Immunol. , vol.19 , pp. 283-291
    • Dooper, M.M.1    Plassen, C.2    Holden, L.3    Lindvik, H.4    Fæste, C.K.5
  • 98
    • 0000354436 scopus 로고
    • The role of cysteine proteinase and carboxypeptidase in the breakdown of storage proteins in buckwheat seeds
    • Dunaevsky, Y. E., and M. A. Belozersky. 1989. The role of cysteine proteinase and carboxypeptidase in the breakdown of storage proteins in buckwheat seeds. Planta 179:316-322.
    • (1989) Planta , vol.179 , pp. 316-322
    • Dunaevsky, Y.E.1    Belozersky, M.A.2
  • 101
    • 58149383790 scopus 로고    scopus 로고
    • Quantitative matrix-assisted laser desorption/ionization mass spectrometry
    • Duncan, M. W., H. Roder, and S. W. Hunsucker. 2008. Quantitative matrix-assisted laser desorption/ionization mass spectrometry. Brief. Funct. Genomics Proteomics 7:355-370.
    • (2008) Brief. Funct. Genomics Proteomics , vol.7 , pp. 355-370
    • Duncan, M.W.1    Roder, H.2    Hunsucker, S.W.3
  • 102
    • 84986531881 scopus 로고
    • Rapid separation and detection of concanavalin a reacting glycoproteins: Application to storage proteins of a legume seed
    • Duranti, M., S. Gorinstein, and P. Cerletti. 1990. Rapid separation and detection of concanavalin A reacting glycoproteins: application to storage proteins of a legume seed. J. Food Biochem. 14:327-330.
    • (1990) J. Food Biochem. , vol.14 , pp. 327-330
    • Duranti, M.1    Gorinstein, S.2    Cerletti, P.3
  • 104
    • 0034640447 scopus 로고    scopus 로고
    • Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high-performance liquid chromatography on polystyrene-divinylbenzene
    • DOI 10.1016/S0021-9673(00)00288-0, PII S0021967300002880
    • Elgar, D. F., C. S. Norris, J. S. Ayers, M. Pritchard, D. E. Otter, and K. P. Palmano. 2000. Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high-performance liquid chromatography on polystyrene- divinylbenzene. J. Chromatogr. A 878:183-196. (Pubitemid 30256135)
    • (2000) Journal of Chromatography A , vol.878 , Issue.2 , pp. 183-196
    • Elgar, D.F.1    Norris, C.S.2    Ayers, J.S.3    Pritchard, M.4    Otter, D.E.5    Palmano, K.P.6
  • 105
    • 0001574606 scopus 로고
    • Amino acid analysis of feedstuff hydrolysates by precolumn derivatization with phenylisothiocyanate and reversed-phase high-performance liquid chromatography
    • Elkin, R. G., and A. M. Wasynczuk. 1987. Amino acid analysis of feedstuff hydrolysates by precolumn derivatization with phenylisothiocyanate and reversed-phase high-performance liquid chromatography. Cereal Chem. 64:226-229.
    • (1987) Cereal Chem. , vol.64 , pp. 226-229
    • Elkin, R.G.1    Wasynczuk, A.M.2
  • 106
    • 20644436694 scopus 로고
    • Fast detection of added soybean proteins in cow's, goat's, and ewe's milk by perfusion reversed-phase high-performance liquid chromatography
    • Espeja, E., M. C. García, and M. L. Marina. 1994. Fast detection of added soybean proteins in cow's, goat's, and ewe's milk by perfusion reversed-phase high-performance liquid chromatography. J. Sep. Sci. 24:856-864.
    • (1994) J. Sep. Sci. , vol.24 , pp. 856-864
    • Espeja, E.1    García, M.C.2    Marina, M.L.3
  • 107
    • 77952776876 scopus 로고    scopus 로고
    • Differentiating cross-reacting allergens in the immunological analysis of celery (Apium graveolens) by mass spectrometry
    • Fæste, C. K., K. R. Jonscher, L. Sit, J. Klawitter, K. E. Løvberg, and L. H. Moen. 2010. Differentiating cross-reacting allergens in the immunological analysis of celery (Apium graveolens) by mass spectrometry. J. AOAC Int. 93:451-461.
    • (2010) J. AOAC Int. , Issue.93 , pp. 451-461
    • Fæste, C.K.1    Jonscher, K.R.2    Sit, L.3    Klawitter, J.4    Løvberg, K.E.5    Moen, L.H.6
  • 109
    • 64649104514 scopus 로고    scopus 로고
    • S2, β, and k-caseins in water buffalo milk by reverse phase-high performance liquid chromatography and mass spectrometry
    • S2, β, and k-caseins in water buffalo milk by reverse phase-high performance liquid chromatography and mass spectrometry. J. Agric. Food Chem. 57: 2988-2992.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 2988-2992
    • Feligini, M.1    Bonizzi, I.2    Buffoni, J.N.3    Cosenza, G.4    Ramunno, L.5
  • 110
    • 0036038834 scopus 로고    scopus 로고
    • A novel antimicrobial function for a ribosomal peptide from rainbow trout skin
    • DOI 10.1016/S0006-291X(02)00837-9, PII S0006291X02008379
    • Fernandes, J. M. O., and V. J. Smith. 2002. A novel antimicrobial function for a ribosomal peptide from rainbow trout skin. Biochem. Biophys. Res. Commun. 296:167-171. (Pubitemid 35002073)
    • (2002) Biochemical and Biophysical Research Communications , vol.296 , Issue.1 , pp. 167-171
    • Fernandes J.M.O1    Smith, V.J.2
  • 111
    • 0035096881 scopus 로고    scopus 로고
    • Mass spectrometry-based procedure for the identification of ovine casein heterogeneity
    • DOI 10.1017/S0022029900004611
    • Ferranti, B. P., R. Pizzano, G. Garro, S. Caira, L. Chianese, and F. Addeo. 2001. Mass spectrometry-based procedure for the identification of ovine casein heterogeneity. J. Dairy Res. 68:35-51. (Pubitemid 32228419)
    • (2001) Journal of Dairy Research , vol.68 , Issue.1 , pp. 35-51
    • Ferranti, P.1    Pizzano, R.2    Garro, G.3    Caira, S.4    Chianese, L.5    Addeo, F.6
  • 112
    • 0031530346 scopus 로고    scopus 로고
    • Combined high resolution chromatographic techniques (FPLC and HPLC) and mass spectrometry-based identification of peptides and proteins in Grana Padano cheese
    • Ferranti, P., E. Itolli, F. Barone, A. Malorni, G. Garro, P. Laezza, L. Chianese, F. Migliaccio, V. Stingo, and F. Addeo. 1997. Combined high resolution chromatographic techniques (FPLC and HPLC) and mass spectrometry-based identification of peptides and proteins in Grana Padano cheese. Lait 77:683-697. (Pubitemid 127387641)
    • (1997) Lait , vol.77 , Issue.6 , pp. 683-697
    • Ferranti, P.1    Itolli, E.2    Barone, F.3    Malorni, A.4    Garro, G.5    Laezza, P.6    Chianese, L.7    Migliaccio, F.8    Stingo, V.9    Addeo, F.10
  • 113
    • 38149045956 scopus 로고    scopus 로고
    • Mass spectrometry analysis of gliadins in celiac disease
    • Ferranti, P., G. Mamone, G. Picariello, and F. Addeo. 2007. Mass spectrometry analysis of gliadins in celiac disease. J. Mass Spectrom. 42:1531-1548.
    • (2007) J. Mass Spectrom. , vol.42 , pp. 1531-1548
    • Ferranti, P.1    Mamone, G.2    Picariello, G.3    Addeo, F.4
  • 114
    • 0141720327 scopus 로고    scopus 로고
    • Detection and quantification of bovine, ovine and caprine milk percentages in protected denomination of origin cheeses by reversed-phase high-performance liquid chromatography of beta-lactoglobulins
    • DOI 10.1016/S0021-9673(03)01261-5
    • Ferreira, I. M., and H. Caçote. 2003. Detection and quantification of bovine, ovine and caprine milk percentages in protected denomination of origin cheeses by reversed-phase high-performance liquid chromatography of beta-lactoglobulins. J. Chromatogr. A 1015: 111-118. (Pubitemid 37168090)
    • (2003) Journal of Chromatography A , vol.1015 , Issue.1-2 , pp. 111-118
    • Ferreira, I.M.P.L.1    Cacote, H.2
  • 116
    • 0033773046 scopus 로고    scopus 로고
    • Use of a single method in the extraction of the seed storage globulins from several legume species. Application to analyse structural comparisons within the major classes of globulins
    • Freitas, R. L., R. B. Ferreira, and A. R. Teixeira. 2000. Use of a single method in the extraction of the seed storage globulins from several legume species. Application to analyse structural comparisons within the major classes of globulins. Int. J. Food Sci. Nutr. 51:341-352.
    • (2000) Int. J. Food Sci. Nutr. , vol.51 , pp. 341-352
    • Freitas, R.L.1    Ferreira, R.B.2    Teixeira, A.R.3
  • 117
    • 4043140026 scopus 로고    scopus 로고
    • Identification and characterization of a new β-casein variant in goat milk by high-performance liquid chromatography with electrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry
    • DOI 10.1002/rcm.1575
    • Galliano, F., R. Saletti, V. Cunsolo, S. Foti, D. Marletta, S. Bordonaro, and G. D'Urso. 2004. Identification and characterization of a new beta-casein variant in goat milk by high-performance liquid chromatography with electrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 18:1972-1982. (Pubitemid 39079175)
    • (2004) Rapid Communications in Mass Spectrometry , vol.18 , Issue.17 , pp. 1972-1982
    • Galliano, F.1    Saletti, R.2    Cunsolo, V.3    Foti, S.4    Marletta, D.5    Bordonaro, S.6    D'Urso, G.7
  • 118
    • 0033771312 scopus 로고    scopus 로고
    • Twodimensional gel electrophoresis/matrix-assisted laser desorption/ ionisation mass spectrometry of a milk powder
    • Galvani, M., M. Hamdan, and P. G. Righetti. 2000. Twodimensional gel electrophoresis/matrix-assisted laser desorption/ ionisation mass spectrometry of a milk powder. Rapid Commun. Mass Spectrom. 14:1889-1897.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1889-1897
    • Galvani, M.1    Hamdan, M.2    Righetti, P.G.3
  • 119
    • 0035096205 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis/matrix-assisted laser desorption/ionisation mass spectrometry of commercial bovine milk
    • DOI 10.1002/rcm.220
    • Galvani, M., M. Hamdan, and P. G. Righetti. 2001. Twodimensional gel electrophoresis/matrix-assisted laser desorption/ ionisation mass spectrometry of commercial bovine milk. Rapid Commun. Mass Spectrom. 15:258-264. (Pubitemid 32201559)
    • (2001) Rapid Communications in Mass Spectrometry , vol.15 , Issue.4 , pp. 258-264
    • Galvani, M.1    Hamdan, M.2    Righetti, P.G.3
  • 120
    • 77949385165 scopus 로고    scopus 로고
    • Characterization and comparative analysis of wheat high molecular weight glutenin subunits by SDS-PAGE, RP-HPLC, HPCE, and MALDI-TOF-MS
    • Gao, L., W. Ma, J. Chen, K. Wang, J. Li, S. Wang, F. Bekes, R. Appels, and Y. Yan. 2010. Characterization and comparative analysis of wheat high molecular weight glutenin subunits by SDS-PAGE, RP-HPLC, HPCE, and MALDI-TOF-MS. J. Agric. Food Chem. 58:2777-2786.
    • (2010) J. Agric. Food Chem. , Issue.58 , pp. 2777-2786
    • Gao, L.1    Ma, W.2    Chen, J.3    Wang, K.4    Li, J.5    Wang, S.6    Bekes, F.7    Appels, R.8    Yan, Y.9
  • 121
    • 26444450533 scopus 로고    scopus 로고
    • The effect of the mobile phase additives on sensitivity in the analysis of peptides and proteins by high-performance liquid chromatography-electrospray mass spectrometry
    • DOI 10.1016/j.jchromb.2005.03.041, PII S1570023205002461, Improving Sensitivity in Liquid Chromatography-Mass Spectrometry
    • García, M. C. 2005. The effect of the mobile phase additives on sensitivity in the analysis of peptides and proteins by highperformance liquid chromatography-electrospray mass spectrometry. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 825:111-123. (Pubitemid 41423594)
    • (2005) Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences , vol.825 , Issue.2 , pp. 111-123
    • Garcia, M.C.1
  • 122
    • 34047168007 scopus 로고    scopus 로고
    • Simple and rapid characterization of soybean cultivars by perfusion reversed-phase HPLC: Application to the estimation of the 11S and 7S globulin contents
    • DOI 10.1002/jssc.200600276
    • García, M. C., J. M. Heras, and M. L. Marina. 2007. Simple and rapid characterization of soybean cultivars by perfusion reversedphase HPLC: application to the estimation of the 11S and 7S globulin contents. J. Sep. Sci. 30:475-482. (Pubitemid 46510561)
    • (2007) Journal of Separation Science , vol.30 , Issue.4 , pp. 475-482
    • Garcia, M.C.1    Heras, J.M.2    Marina, M.L.3
  • 123
    • 33645126334 scopus 로고    scopus 로고
    • Rapid detection of the addition of soybean proteins to cheese and other dairy products by reversed-phase perfusion chromatography
    • García, M. C., and M. L. Marina. 2006. Rapid detection of the addition of soybean proteins to cheese and other dairy products by reversed-phase perfusion chromatography. Food Addit. Contam. 23: 339-347.
    • (2006) Food Addit. Contam. , vol.23 , pp. 339-347
    • García, M.C.1    Marina, M.L.2
  • 124
    • 0031683067 scopus 로고    scopus 로고
    • Ultrarapid detection of bovine whey proteins in powdered soybean milk by perfusion reversed-phase high-performance liquid chromatography
    • DOI 10.1016/S0021-9673(98)00619-0, PII S0021967398006190
    • García, M. C., M. L. Marina, and M. Torre. 1998. Ultrarapid detection of bovine whey proteins in powdered soybean milk by perfusion reversed-phase high-performance liquid chromatography. J. Chromatogr. A 822:225-232. (Pubitemid 28461927)
    • (1998) Journal of Chromatography A , vol.822 , Issue.2 , pp. 225-232
    • Garcia, M.C.1    Marina, M.L.2    Torre, M.3
  • 125
    • 0031561768 scopus 로고    scopus 로고
    • Rapid separation of soybean globulins by reversed-phase high-performance liquid chromatography
    • DOI 10.1016/S0021-9673(96)00717-0, PII S0021967396007170
    • García, M. C., M. Torre, F. Laborda, and M. L. Marina. 1997. Rapid separation of soybean globulins by reversed-phase highperformance liquid chromatography. J. Chromatogr. A 758: 75-83. (Pubitemid 27056138)
    • (1997) Journal of Chromatography A , vol.758 , Issue.1 , pp. 75-83
    • Garcia, M.C.1    Torre, M.2    Laborda, F.3    Marina, M.L.4
  • 126
    • 0034625589 scopus 로고    scopus 로고
    • Characterization of commercial soybean products by conventional and perfusion reversed-phase high-performance liquid chromatography and multivariate analysis
    • DOI 10.1016/S0021-9673(99)01279-0, PII S0021967399012790
    • García, M. C., M. Torre, and M. L. Marina. 2000. Characterization of commercial soybean products by conventional and perfusion reversed-phase high-performance liquid chromatography and multivariate analysis. J. Chromatogr. A 881:47-57. (Pubitemid 30332192)
    • (2000) Journal of Chromatography A , vol.881 , Issue.1-2 , pp. 47-57
    • Garcia, M.C.1    Torre, M.2    Marina, M.L.3
  • 127
    • 0034595911 scopus 로고    scopus 로고
    • Perfusion chromatography: An emergent technique for the analysis of food proteins
    • DOI 10.1016/S0021-9673(00)00354-X, PII S002196730000354X
    • García, M. C., M. Torre, and M. L. Marina. 2000. Perfusion chromatography: an emergent technique for the analysis of food proteins. J. Chromatogr. A 880:169-187. (Pubitemid 30317302)
    • (2000) Journal of Chromatography A , vol.880 , Issue.1-2 , pp. 169-187
    • Garcia, M.C.1    Marina, M.L.2    Torre, M.3
  • 129
    • 0032722261 scopus 로고    scopus 로고
    • Use of hydroxyacetophenones as matrices for the analysis of high molecular weight glutenin mixtures by matrix-assisted laser desorption/ ionization mass spectrometry
    • DOI 10.1002/(SICI)1097-0231(19991115)13:21<2084::AID-RCM757>3.0. CO;2-6
    • Garozzo, D., R. Cozzolino, S. Di Giorgi, S. Fisichella, and D. Lafiandra. 1999. Use of hydroxyacetophenones as matrices for the analysis of high molecular weight glutenin mixtures by matrixassisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 13:2084-2089. (Pubitemid 29514392)
    • (1999) Rapid Communications in Mass Spectrometry , vol.13 , Issue.21 , pp. 2084-2089
    • Garozzo, D.1    Cozzolino, R.2    Di Giorgi, S.3    Fisichella, S.4    Lafiandra, D.5
  • 130
    • 37549056273 scopus 로고    scopus 로고
    • Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis
    • Gaur, V., D. K. Sethi, and D. M. Salunke. 2008. Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis. Acta Cryst. F64: 32-35.
    • (2008) Acta Cryst. F , vol.64 , pp. 32-35
    • Gaur, V.1    Sethi, D.K.2    Salunke, D.M.3
  • 131
    • 0037229145 scopus 로고    scopus 로고
    • A proteomic investigation of isolated soy proteins with variable effects in experimental and clinical studies
    • Gianazza, E., I. Eberini, A. Arnoldi, R. Wait, and C. R. Sirtori. 2003. A proteomic investigation of isolated soy proteins with variable effects in experimental and clinical studies. J. Nutr. 133:9-14. (Pubitemid 36070569)
    • (2003) Journal of Nutrition , vol.133 , Issue.1 , pp. 9-14
    • Gianazza, E.1    Eberini, I.2    Arnoldi, A.3    Wait, R.4    Sirtori, C.R.5
  • 132
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by
    • Gobom, J., E. Nordhoff, E. Mirgorodskaya, R. Ekman, and P. Roepstorff. 1999. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 34: 105-116.
    • (1999) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 133
    • 0035253337 scopus 로고    scopus 로고
    • Alpha-cyano-4-hydroxycinnamic acid affinity sample preparation. A protocol for MALDI-MS peptide analysis in proteomics
    • Gobom, J., M. Schuerenberg, M. Mueller, D. Theiss, H. Lehrach, and E. Nordhoff. 2001. Alpha-cyano-4-hydroxycinnamic acid affinity sample preparation. A protocol for MALDI-MS peptide analysis in proteomics. Anal. Chem. 73:434-438.
    • (2001) Anal. Chem. , vol.73 , pp. 434-438
    • Gobom, J.1    Schuerenberg, M.2    Mueller, M.3    Theiss, D.4    Lehrach, H.5    Nordhoff, E.6
  • 134
    • 33646255916 scopus 로고    scopus 로고
    • An ecotoxicoproteomic approach (SELDI-TOF mass spectrometry) to biomarker discovery in crab exposed to pollutants under laboratory conditions
    • Gomiero, A., D. M. Pampanin, A. Bjørnstad, B. K. Larsen, F. Provan, E. Lyng, and O. K. Andersen. 2006. An ecotoxicoproteomic approach (SELDI-TOF mass spectrometry) to biomarker discovery in crab exposed to pollutants under laboratory conditions. Aquat. Toxicol. 78:S34-S41.
    • (2006) Aquat. Toxicol. , vol.78
    • Gomiero, A.1    Pampanin, D.M.2    Bjørnstad, A.3    Larsen, B.K.4    Provan, F.5    Lyng, E.6    Andersen, O.K.7
  • 139
    • 26444456180 scopus 로고    scopus 로고
    • Application of mass spectrometry in proteomics
    • DOI 10.1007/s10540-005-2849-x
    • Guerrera, I. C., and O. Kleiner. 2005. Application of mass spectrometry in proteomics. Biosci. Rep. 25:71-93. (Pubitemid 41437711)
    • (2005) Bioscience Reports , vol.25 , Issue.1-2 , pp. 71-93
    • Guerrera, I.C.1    Kleiner, O.2
  • 141
    • 0035847245 scopus 로고    scopus 로고
    • Protein-based chiral stationary phases for highperformance liquid chromatography enantioseparations
    • Haginaka, J. 2001. Protein-based chiral stationary phases for highperformance liquid chromatography enantioseparations. J. Chromatogr. A 906:253-273.
    • (2001) J. Chromatogr.A , vol.906 , pp. 253-273
    • Haginaka, J.1
  • 142
    • 20444449370 scopus 로고    scopus 로고
    • A systematic proteomic study of seed filling in soybean. Establishment of high-resolution two-dimensional reference maps, expression profiles, and an interactive proteome database
    • DOI 10.1104/pp.104.056614
    • Hajduch, M., A. Ganapathy, J. W. Stein, and J. J. Thelen. 2005. A systematic proteomic study of seed filling in soybean. establishment of high-resolution two-dimensional reference maps, expression profiles, and an interactive proteome database. Plant Physiol. 137: 1397-1419. (Pubitemid 43119338)
    • (2005) Plant Physiology , vol.137 , Issue.4 , pp. 1397-1419
    • Hajduch, M.1    Ganapathy, A.2    Stein, J.W.3    Thelen, J.J.4
  • 144
    • 0035839263 scopus 로고    scopus 로고
    • Characterisation of modified whey protein in milk ingredients by liquid chromatography coupled to electrospray ionisation mass spectrometry
    • DOI 10.1016/S0021-9673(01)00710-5, PII S0021967301007105
    • Hau, J., and L. Bovetto. 2001. Characterisation of modified whey protein in milk ingredients by liquid chromatography coupled to electrospray ionisation mass spectrometry. J. Chromatogr. A 926: 105-112. (Pubitemid 32739011)
    • (2001) Journal of Chromatography A , vol.926 , Issue.1 , pp. 105-112
    • Hau, J.1    Bovetto, L.2
  • 145
    • 0036006646 scopus 로고    scopus 로고
    • Heat-induced covalent complex between casein micelles and β-lactoglobulin from goat's milk: Identification of an involved disulfide bond
    • DOI 10.1021/jf010625w
    • Henry, G., D. Mollé, F. Morgan, J. Fauquant, and S. Bouhallab. 2002. Heat-induced covalent complex between casein micelles and beta-lactoglobulin from goat's milk: identification of an involved disulfide bond. J. Agric. Food Chem. 50:185-191. (Pubitemid 34038529)
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.1 , pp. 185-191
    • Henry, G.1    Molle, D.2    Morgan, F.3    Fauquant, J.4    Bouhallab, S.5
  • 146
    • 34248525383 scopus 로고    scopus 로고
    • Development of a perfusion ion-exchange chromatography method for the separation of soybean proteins and its application to cultivar characterization
    • DOI 10.1016/j.chroma.2006.12.052, PII S0021967306023892, Advances in Sample Preparation Part II
    • Heras, J. M., M. L. Marina, and M. C. García. 2007. Development of a perfusion ion-exchange chromatography method for the separation of soybean proteins and its application to cultivar characterization. J. Chromatogr. A 1153:97-103. (Pubitemid 46755186)
    • (2007) Journal of Chromatography A , vol.1153 , Issue.1-2 , pp. 97-103
    • Heras, J.M.1    Marina, M.L.2    Garcia, M.C.3
  • 147
    • 0042856251 scopus 로고    scopus 로고
    • New strategy for the determination of gliadins in maize- or rice-based foods matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: Fractionation of gliadins from maize or rice prolamins by acidic treatment
    • DOI 10.1002/jms.502
    • Hernando, A., I. Valdes, and E. Méndez. 2003. New strategy for the determination of gliadins in maize-or rice-based foods matrixassisted laser desorption/ionization time-of-flight mass spectrometry: fractionation of gliadins from maize or rice prolamins by acidic treatment. J. Mass Spectrom. 38:862-871. (Pubitemid 37062953)
    • (2003) Journal of Mass Spectrometry , vol.38 , Issue.8 , pp. 862-871
    • Hernando, A.1    Valdes, I.2    Mendez, E.3
  • 148
    • 85025567093 scopus 로고
    • Detection of soy milk in pasteurised bovine milk
    • Hewedy, M. M., and C. J. Smith. 1989. Detection of soy milk in pasteurised bovine milk. Food Hydrocolloids 3:399-405.
    • (1989) Food Hydrocolloids , vol.3 , pp. 399-405
    • Hewedy, M.M.1    Smith, C.J.2
  • 149
    • 0001589833 scopus 로고
    • Molecular weights of high molecular weight subunits of glutenin determined by mass spectrometry
    • Hickman, D. R., P. Roepstorff, P. R. Shewry, and A. S. Tatham. 1995. Molecular weights of high molecular weight subunits of glutenin determined by mass spectrometry. J. Cereal Sci. 22:99-103.
    • (1995) J. Cereal Sci. , vol.22 , pp. 99-103
    • Hickman, D.R.1    Roepstorff, P.2    Shewry, P.R.3    Tatham, A.S.4
  • 150
    • 0036834966 scopus 로고    scopus 로고
    • Comparison of peptides in the phloem sap of flowering and non-flowering Perilla and lupine plants using microbore HPLC followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • DOI 10.1007/s00425-002-0916-0
    • Hoffmann-Benning, S., D. A. Gage, L. McIntosh, H. Kende, and J. A. D. Zeevaart. 2002. Comparison of peptides in the phloem sap of flowering and non-flowering Perilla and lupine plants using microbore HPLC followed by matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry. Planta 216:140-147. (Pubitemid 36761557)
    • (2002) Planta , vol.216 , Issue.1 , pp. 140-147
    • Hoffmann-Benning, S.1    Gage, D.A.2    McIntosh, L.3    Kende, H.4    Zeevaart, J.A.D.5
  • 151
    • 0036897967 scopus 로고    scopus 로고
    • Application of genomics and proteomics for study of the integrated response to zinc exposure in a non-model fish species, the rainbow trout
    • DOI 10.1016/S1096-4959(02)00125-2, PII S1096495902001252
    • Hogstrand, C., S. Balesaria, and C. N. Glover. 2002. Application of genomics and proteomics for study of the integrated response to zinc exposure in a non-model fish species, the rainbow trout. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 133:523-535. (Pubitemid 35441079)
    • (2002) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology , vol.133 , Issue.4 , pp. 523-535
    • Hogstrand, C.1    Balesaria, S.2    Glover, C.N.3
  • 152
    • 38049079212 scopus 로고    scopus 로고
    • Fast characterization of industrial soy protein isolates by direct analysis with matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • Horneffer, V., T. J. Foster, and K. P. Velikov. 2007. Fast characterization of industrial soy protein isolates by direct analysis with matrix-assisted laser desorption ionization time-of-flight mass spectrometry. J. Agric. Food Chem. 55:10505-10508.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 10505-10508
    • Horneffer, V.1    Foster, T.J.2    Velikov, K.P.3
  • 153
    • 0033004874 scopus 로고    scopus 로고
    • Evaluation of volatile eluents and electrolytes for high-performance liquid chromatography-electrospray ionization mass spectrometry and capillary electrophoresis-electrospray ionization mass spectrometry of proteins I. Liquid chromatography
    • DOI 10.1016/S0021-9673(99)00532-4, PII S0021967399005324
    • Huber, C. G., and A. Premstaller. 1999. Evaluation of volatile eluents and electrolytes for high-performance liquid chromatography-electrospray ionization mass spectrometry and capillary electrophoresis-electrospray ionization mass spectrometry of proteins I. Liquid chromatography. J. Chromatogr. A 849:161-173 (Pubitemid 29301664)
    • (1999) Journal of Chromatography A , vol.849 , Issue.1 , pp. 161-173
    • Huber, C.G.1    Premstaller, A.2
  • 154
    • 57149106279 scopus 로고    scopus 로고
    • Effect of high temperature on albumin and globulin accumulation in the endosperm proteome of the developing wheat grain
    • Hurkman, W. J., W. H. Vensel, C. K. Tanaka, L. Whitehand, and S. B. Altenbach. 2009. Effect of high temperature on albumin and globulin accumulation in the endosperm proteome of the developing wheat grain. J. Cereal Sci. 49:12-23.
    • (2009) J. Cereal Sci. , vol.49 , pp. 12-23
    • Hurkman, W.J.1    Vensel, W.H.2    Tanaka, C.K.3    Whitehand, L.4    Altenbach, S.B.5
  • 155
    • 0001747255 scopus 로고
    • Purification and properties of the trypsin inhibitors from buckwheat seed
    • Ikeda, K., and T. Kusano. 1983. Purification and properties of the trypsin inhibitors from buckwheat seed. Agric. Biol. Chem. 47: 1481-1486.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 1481-1486
    • Ikeda, K.1    Kusano, T.2
  • 156
    • 0002602221 scopus 로고
    • Alpha-amylase inhibitor in buckwheat seed
    • Ikeda, K., K. Shida, and M. Kishida. 1994. Alpha-amylase inhibitor in buckwheat seed. Fagopyrum 14:3-6.
    • (1994) Fagopyrum , vol.14 , pp. 3-6
    • Ikeda, K.1    Shida, K.2    Kishida, M.3
  • 157
    • 0024980938 scopus 로고
    • Complete amino acid sequence of the sarcoplasmic calcium-binding protein (SCP-I) from crayfish (Astacus leptodactylus)
    • Jauregui-Adell, J., W. Wnuk, and J. A. Cox. 1989. Complete amino acid sequence of the sarcoplasmic calcium-binding protein (SCP-I) from crayfish (Astacus leptodactylus). FEBS Lett. 243:209-212.
    • (1989) FEBS Lett. , vol.243 , pp. 209-212
    • Jauregui-Adell, J.1    Wnuk, W.2    Cox, J.A.3
  • 158
    • 0032603342 scopus 로고    scopus 로고
    • Sample preparation methods for mass spectrometric peptide mapping directly from 2-DE gels
    • Jensen, O. N., M. Wilm, A. Shevchenko, and M. Mann. 1999. Sample preparation methods for mass spectrometric peptide mapping directly from 2-DE gels. Methods Mol. Biol. 112:513-530.
    • (1999) Methods Mol. Biol. , vol.112 , pp. 513-530
    • Jensen, O.N.1    Wilm, M.2    Shevchenko, A.3    Mann, M.4
  • 159
    • 34548417649 scopus 로고    scopus 로고
    • Plant proteome analysis: A 2006 update
    • DOI 10.1002/pmic.200700135
    • Jorrín, J. V., A. M. Maldonado, and M. A. Castillejo. 2007. Plant proteome analysis: a 2006 update. Proteomics 7:2947-2962. (Pubitemid 47359932)
    • (2007) Proteomics , vol.7 , Issue.16 , pp. 2947-2962
    • Jorrn, J.V.1    Maldonado, A.M.2    Castillejo, Ma.A.3
  • 160
    • 34250895759 scopus 로고    scopus 로고
    • Proteomic studies on protein oxidation in bonito (Katsuwonus pelamis) muscle
    • DOI 10.3136/fstr.13.133
    • Kinoshita, Y., T. Sato, H. Naitou, N. Ohashi, and S. Kumazawa. 2007. Proteomic studies on protein oxidation in bonito (Katsuwonus pelamis) muscle. Food Sci. Technol. Res. 13:133-138. (Pubitemid 46986830)
    • (2007) Food Science and Technology Research , vol.13 , Issue.2 , pp. 133-138
    • Kinoshita, Y.1    Sato, T.2    Naitou, H.3    Ohashi, N.4    Kumazawa, S.5
  • 162
    • 33645082204 scopus 로고    scopus 로고
    • Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis
    • Kjaersgård, I. V., M. R. Nørrelykke, and F. Jessen. 2006. Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis. Proteomics 6:1606-1618.
    • (2006) Proteomics , vol.6 , pp. 1606-1618
    • Kjaersgård, I.V.1    Nørrelykke, M.R.2    Jessen, F.3
  • 163
    • 4444349745 scopus 로고    scopus 로고
    • Surface-enhanced laser desorption/ionization-time of flight-mass spectrometry approach to biomarker discovery in blue mussels (Mytilus edulis) exposed to polyaromatic hydrocarbons and heavy metals under field conditions
    • DOI 10.1002/pmic.200300828
    • Knigge, T., T. Monsinjon, and O. K. Andersen. 2004. Surfaceenhanced laser desorption/ionization-time of flight-mass spectrometry approach to biomarker discovery in blue mussels (Mytilus edulis) exposed to polyaromatic hydrocarbons and heavy metals under field conditions. Proteomics 4:2722-2727. (Pubitemid 39206317)
    • (2004) Proteomics , vol.4 , Issue.9 , pp. 2722-2727
    • Knigge, T.1    Monsinjon, T.2    Andersen, O.-K.3
  • 164
    • 0032559403 scopus 로고    scopus 로고
    • Identification of fish species by reversed-phase high-performance liquid chromatography with photodiode-array detection
    • DOI 10.1016/S0378-4347(97)00505-7, PII S0378434797005057
    • Knuutinen, J., and P. Harjula. 1998. Identification of fish species by reversed-phase high-performance liquid chromatography with photodiode-array detection. J. Chromatogr. B 705:11-21. (Pubitemid 28045650)
    • (1998) Journal of Chromatography B: Biomedical Applications , vol.705 , Issue.1 , pp. 11-21
    • Knuutinen, J.1    Harjula, P.2
  • 166
    • 61449146289 scopus 로고    scopus 로고
    • All three subunits of soybean b-conglycinin are potential food allergens
    • Krishnan, H. B., W. S. Kim, S. Jang, and M. S. Kerley. 2009. All three subunits of soybean b-conglycinin are potential food allergens. J. Agric. Food Chem. 57:938-943.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 938-943
    • Krishnan, H.B.1    Kim, W.S.2    Jang, S.3    Kerley, M.S.4
  • 167
    • 67649184776 scopus 로고    scopus 로고
    • A rapid and simple procedure for the depletion of abundant storage proteins from legume seeds to advance proteome analysis: A case study using Glycine max
    • Krishnan, H. B., N. W. Oehrle, and S. S. Natarajan. 2009. A rapid and simple procedure for the depletion of abundant storage proteins from legume seeds to advance proteome analysis: a case study using Glycine max. Proteomics 9:3174-3188.
    • (2009) Proteomics , vol.9 , pp. 3174-3188
    • Krishnan, H.B.1    Oehrle, N.W.2    Natarajan, S.S.3
  • 168
    • 0034655767 scopus 로고    scopus 로고
    • A reversed-phase high-performance liquid chromatographic method for the determination of soya bean proteins in bovine milks
    • DOI 10.1021/ac990776m
    • Kruså, M., M. Torre, and M. L. Marina. 2000. A reversed-phase high-performance liquid chromatographic method for the determination of soya bean proteins in bovine milks. Anal. Chem. 72:1814-1818. (Pubitemid 30220175)
    • (2000) Analytical Chemistry , vol.72 , Issue.8 , pp. 1814-1818
    • Krusa, M.1    Torre, M.2    Marina, Ma.L.3
  • 171
    • 33646252476 scopus 로고    scopus 로고
    • Comparison of protein expression in plasma from nonylphenol and bisphenol A-exposed Atlantic cod (Gadus morhua) and turbot (Scophthalmus maximus) by use of SELDI-TOF
    • Larsen, B. K., A. Bjørnstad, R. C. Sundt, I. C. Taban, D. M. Pampanin, and O. K. Andersen. 2006. Comparison of protein expression in plasma from nonylphenol and bisphenol A-exposed Atlantic cod (Gadus morhua) and turbot (Scophthalmus maximus) by use of SELDI-TOF. Aquat. Toxicol. 78:S25-S33.
    • (2006) Aquat. Toxicol. , vol.78
    • Larsen, B.K.1    Bjørnstad, A.2    Sundt, R.C.3    Taban, I.C.4    Pampanin, D.M.5    Andersen, O.K.6
  • 173
    • 7444229728 scopus 로고    scopus 로고
    • Hazelnut (Corylus avellana) vicilin Cor a 11: Molecular characterization of a glycoprotein and its allergenic activity
    • DOI 10.1042/BJ20041062
    • Lauer, I., K. Foetisch, D. Kolarich, B. K. Ballmer-Weber, A. Conti, F. Altmann, S. Vieths, and S. Scheurer. 2004. Hazelnut (Corylus avellana) vicilin Cor a 11: molecular characterization of a glycoprotein and its allergenic activity. Biochem. J. 383:327-334. (Pubitemid 39446694)
    • (2004) Biochemical Journal , vol.383 , Issue.2 , pp. 327-334
    • Lauer, I.1    Foetisch, K.2    Kolarich, D.3    Ballmer-Weber, B.K.4    Conti, A.5    Altmann, F.6    Vieths, S.7    Scheurer, S.8
  • 174
    • 84985200262 scopus 로고    scopus 로고
    • Separation of cod (Gadus morhua) fillet proteins by electrophoresis and HPLC after various frozen storage treatments
    • LeBlanc, E. L., and R. J. LeBlanc. 2006. Separation of cod (Gadus morhua) fillet proteins by electrophoresis and HPLC after various frozen storage treatments. J. Food Sci. 54:827-834.
    • (2006) J. Food Sci. , vol.54 , pp. 827-834
    • LeBlanc, E.L.1    LeBlanc, R.J.2
  • 175
    • 77952773738 scopus 로고    scopus 로고
    • Determination of allergenic egg proteins in food by protein-, mass spectrometry-, and DNA-based methods
    • Lee, J.-Y., and C.-J. Kim. 2010. Determination of allergenic egg proteins in food by protein-, mass spectrometry-, and DNA-based methods. J. AOAC Int. 93:462-477.
    • (2010) J. AOAC Int. , vol.93 , pp. 462-477
    • Lee, J.-Y.1    Kim, C.-J.2
  • 176
    • 0344494027 scopus 로고    scopus 로고
    • Applications of affinity chromatography in proteomics
    • DOI 10.1016/j.ab.2003.08.031
    • Lee, W.-C., and K. H. Lee. 2004. Applications of affinity chromatography in proteomics. Anal. Biochem. 324:1-10. (Pubitemid 37491116)
    • (2004) Analytical Biochemistry , vol.324 , Issue.1 , pp. 1-10
    • Lee, W.-C.1    Lee, K.H.2
  • 177
    • 33748317825 scopus 로고    scopus 로고
    • Identification of marker proteins for the adulteration of meat products with soybean proteins by multidimensional liquid chromatography-tandem mass spectrometry
    • DOI 10.1021/pr060145q
    • Leitner, A., F. Castro-Rubio, M. L. Marina, and W. Lindner. 2006. Identification of marker proteins for the adulteration of meat products with soybean proteins by multidimensional liquid chromatography-tandem mass spectrometry. J. Proteome Res. 5: 2424-2430. (Pubitemid 44330836)
    • (2006) Journal of Proteome Research , vol.5 , Issue.9 , pp. 2424-2430
    • Leitner, A.1    Castro-Rubio, F.2    Marina, M.L.3    Lindner, W.4
  • 179
    • 0037505302 scopus 로고    scopus 로고
    • Application of chromatography and mass spectrometry to the characterization of food proteins and derived peptides
    • DOI 10.1016/S0021-9673(00)00071-6, PII S0021967300000716
    • Léonil, J., V. Gagnaire, D. Mollé, S. Pezennec, and S. Bouhallab. 2000. Application of chromatography and mass spectrometry to the characterization of food proteins and derived peptides. J. Chromatogr. A 881:1-21. (Pubitemid 30332189)
    • (2000) Journal of Chromatography A , vol.881 , Issue.1-2 , pp. 1-21
    • Leonil, J.1    Gagnaire, V.2    Molle, D.3    Pezennec, S.4    Bouhallab, S.5
  • 180
    • 0031253029 scopus 로고    scopus 로고
    • Characterization by Ionization Mass Spectrometry of Lactosyl β-Lactoglobulin Conjugates Formed during Heat Treatment of Milk and Whey and Identification of One Lactose-Binding Site
    • Léonil, J., D. Mollé, J. Fauquant, J. L. Maubois, R. J. Pearce, and S. Bouhallab. 1997. Characterization by ionization mass spectrometry of lactosyl beta-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactosebinding site. J. Dairy Sci. 80:2270-2281. (Pubitemid 127446920)
    • (1997) Journal of Dairy Science , vol.80 , Issue.10 , pp. 2270-2281
    • Leonil, J.1    Molle, D.2    Fauquant, J.3    Maubois, J.L.4    Pearce, R.J.5    Bouhallab, S.6
  • 181
    • 21844511439 scopus 로고
    • Analysis of major bovine milk proteins by on-line high-performance liquid chromatography and electrospray ionization-mass spectrometry
    • Léonil, J., D. Mollé, F. Gaucheron, P. Arpino, P. Guénot, and J. L. Maubois. 1995. Analysis of major bovine milk proteins by on-line high-performance liquid chromatography and electrospray ionization-mass spectrometry. Lait 75:193-210.
    • (1995) Lait , vol.75 , pp. 193-210
    • Léonil, J.1    Mollé, D.2    Gaucheron, F.3    Arpino, P.4    Guénot, P.5    Maubois, J.L.6
  • 182
    • 0001045321 scopus 로고
    • Characterization of low molecular weight glutenin subunits by reversed-phase high-performance liquid chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and N-terminal amino acid sequencing
    • Lew, E. J.-L., D. D. Kuzmicky, and D. D. Kasarda. 1992. Characterization of low molecular weight glutenin subunits by reversed-phase high-performance liquid chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and N-terminal amino acid sequencing. Cereal Chem. 69:508-515.
    • (1992) Cereal Chem. , vol.69 , pp. 508-515
    • Lew, E.J.-L.1    Kuzmicky, D.D.2    Kasarda, D.D.3
  • 183
    • 0017333814 scopus 로고
    • Application and limitation of isoelectric focusing and high performance chromatography in the estimation of soya proteins in meat products
    • Llewellyn, J. W., and R. Sawyer. 1977. Application and limitation of isoelectric focusing and high performance chromatography in the estimation of soya proteins in meat products. Ann. Nutr. Aliment. 31: 231-232.
    • (1977) Ann. Nutr. Aliment. , vol.31 , pp. 231-232
    • Llewellyn, J.W.1    Sawyer, R.2
  • 184
    • 33645859043 scopus 로고    scopus 로고
    • Preliminary approaches for the development of a high-performance liquid chromatography/electrospray ionization tandem mass spectrometry method for the detection and label-free semi-quantitation of the main storage proteins of Lupinus albus in foods
    • Locati, D., S. Morandi, M. Zanotti, and A. Arnoldi. 2006. Preliminary approaches for the development of a high-performance liquid chromatography/ electrospray ionization tandem mass spectrometry method for the detection and label-free semi-quantitation of the main storage proteins of Lupinus albus in foods. Rapid Commun. Mass Spectrom. 20:1305-1316.
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 1305-1316
    • Locati, D.1    Morandi, S.2    Zanotti, M.3    Arnoldi, A.4
  • 185
    • 0026436330 scopus 로고
    • Multiply charged negative ions by electrospray ionization of polypeptides and proteins
    • Loo, J. A., R. R. Loo, K. J. Light, C. G. Edmonds, and R. D. Smith. 1992. Multiply charged negative ions by electrospray ionization of polypeptides and proteins. Anal. Chem. 64:81-88.
    • (1992) Anal. Chem. , vol.64 , pp. 81-88
    • Loo, J.A.1    Loo, R.R.2    Light, K.J.3    Edmonds, C.G.4    Smith, R.D.5
  • 187
    • 0036907894 scopus 로고    scopus 로고
    • Application of proteomics for fast identification of species-specific peptides from marine species
    • DOI 10.1002/1615-9861(200212)2:12<1658::AID-PROT1658>3.0.CO;2-4
    • López, J. L., A. Marina, G. Alvarez, and J. Vázquez. 2002. Application of proteomics for fast identification of species-specific peptides from marine species. Proteomics 2:1658-1665. (Pubitemid 36015501)
    • (2002) Proteomics , vol.2 , Issue.12 , pp. 1658-1665
    • Lopez, J.L.1    Marina, A.2    Alvarez, G.3    Vazquez, J.4
  • 188
    • 0036934090 scopus 로고    scopus 로고
    • A proteomic approach to the study of the marine mussels Mytilus edulis and M. galloprovincialis
    • DOI 10.1007/s00227-002-0827-4
    • López, J. L., A. Marina, J. Vázquez, and G. Alvarez. 2002. A proteomic approach to the study of the marine mussels Mytilus edulis and M. galloprovincialis. Mar. Biol. 141:217-223. (Pubitemid 36064303)
    • (2002) Marine Biology , vol.141 , Issue.2 , pp. 217-223
    • Lopez, J.L.1    Marina, A.2    Vazquez, J.3    Alvarez, G.4
  • 190
    • 34548040972 scopus 로고    scopus 로고
    • Identification of plant proteins in adulterated skimmed milk powder by high-performance liquid chromatography-mass spectrometry
    • DOI 10.1016/j.chroma.2007.07.017, PII S0021967307012101
    • Luykx, D. M., J. H. Cordewener, P. Ferranti, R. Frankhuizen, M. G. Bremer, H. Hooijerink, and A. H. America. 2007. Identification of plant proteins in adulterated skimmed milk powder by highperformance liquid chromatography-mass spectrometry. J. Chromatogr. A 1164:189-197. (Pubitemid 47284109)
    • (2007) Journal of Chromatography A , vol.1164 , Issue.1-2 , pp. 189-197
    • Luykx, D.M.A.M.1    Cordewener, J.H.G.2    Ferranti, P.3    Frankhuizen, R.4    Bremer, M.G.E.G.5    Hooijerink, H.6    America, A.H.P.7
  • 192
    • 69349093534 scopus 로고    scopus 로고
    • Fractionation and evaluation of radical scavenging peptides from in vitro digests of buckwheat protein
    • Ma, Y., Y. L. Xiong, J. Zhai, H. Zhu, and T. Dziubla. 2010. Fractionation and evaluation of radical scavenging peptides from in vitro digests of buckwheat protein. Food Chem. 118:582-588.
    • (2010) Food Chem. , Issue.118 , pp. 582-588
    • Ma, Y.1    Xiong, Y.L.2    Zhai, J.3    Zhu, H.4    Dziubla, T.5
  • 193
    • 0034283062 scopus 로고    scopus 로고
    • An 18.5 kDa protein from the amebocyte of Limulus polyphemus, homologous to the previously described amebocyte aggregation factor, expresses alternative phospholipase A2 activity
    • MacPherson, J. C., and R. S. Jacobs. 2000. An 18.5 kDa protein from the amebocyte of Limulus polyphemus, homologous to the previously described amebocyte aggregation factor, expresses alternative phospholipase A2 activity. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 127:31-44.
    • (2000) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.127 , pp. 31-44
    • MacPherson, J.C.1    Jacobs, R.S.2
  • 194
    • 33947190376 scopus 로고    scopus 로고
    • Combined 2D electrophoretic approaches for the study of white lupin mature seed storage proteome
    • DOI 10.1016/j.phytochem.2007.01.003, PII S0031942207000258
    • Magni, C., A. Scarafoni, A. Herndl, F. Sessa, B. Prinsi, L. Espen, and M. Duranti. 2007. Combined 2D electrophoretic approaches for the study of white lupin mature seed storage proteome. Phytochemistry 68:997-1007. (Pubitemid 46413333)
    • (2007) Phytochemistry , vol.68 , Issue.7 , pp. 997-1007
    • Magni, C.1    Scarafoni, A.2    Herndl, A.3    Sessa, F.4    Prinsi, B.5    Espen, L.6    Duranti, M.7
  • 195
    • 10044254444 scopus 로고    scopus 로고
    • Conglutin γ, a lupin seed protein, binds insulin in vitro and reduces plasma glucose levels of hyperglycemic rats
    • DOI 10.1016/j.jnutbio.2004.06.009, PII S095528630400141X
    • Magni, C., F. Sessa, E. Accardo, M. Vanoni, P. Morazzoni, A. Scarafoni, and M. Duranti. 2004. Conglutin gamma, a lupin seed protein, binds insulin in vitro and reduces plasma glucose levels of hyperglycemic rats. J. Nutr. Biochem. 15:646-650. (Pubitemid 39611362)
    • (2004) Journal of Nutritional Biochemistry , vol.15 , Issue.11 , pp. 646-650
    • Magni, C.1    Sessa, F.2    Accardo, E.3    Vanoni, M.4    Morazzoni, P.5    Scarafoni, A.6    Duranti, M.7
  • 196
    • 0037330377 scopus 로고    scopus 로고
    • Proteomic analysis of the effect of heat stress on hexaploid wheat grain: Characterization of heat-responsive proteins from total endosperm
    • DOI 10.1002/pmic.200390026
    • Majoul, T., E. Bancel, E. Triboi, J. B. Hamida, and G. Branlard. 2003. Proteomic analysis of the effect of heat stress on hexaploid wheat grain: characterization of heat-responsive proteins from total endosperm. Proteomics 3:175-183. (Pubitemid 36254600)
    • (2003) Proteomics , vol.3 , Issue.2 , pp. 175-183
    • Majoul, T.1    Bancel, E.2    Triboi, E.3    Hamida, J.B.4    Branlard, G.5
  • 197
    • 1242316937 scopus 로고    scopus 로고
    • Proteomic analysis of the effect of heat stress on hexaploid wheat grain: Characterization of heat-responsive proteins from non-prolamins fraction
    • DOI 10.1002/pmic.200300570
    • Majoul, T., E. Bancel, E. Triboi, J. B. Hamida, and G. Branlard. 2004. Proteomic analysis of the effect of heat stress on hexaploid wheat grain: characterization of heat-responsive proteins from nonprolamins fraction. Proteomics 4:505-513. (Pubitemid 38235270)
    • (2004) Proteomics , vol.4 , Issue.2 , pp. 505-513
    • Majoul, T.1    Bancel, E.2    Triboi, E.3    Hamida, J.B.4    Branlard, G.5
  • 198
    • 23044444710 scopus 로고    scopus 로고
    • Characterization of wheat gliadin proteins by combined two-dimensional gel electrophoresis and tandem mass spectrometry
    • DOI 10.1002/pmic.200401168
    • Mamone, G., F. Addeo, L. Chianese, A. Di Luccia, A. De Martino, A. Nappo, A. Formisano, P. De Vivo, and P. Ferranti. 2005. Characterization of wheat gliadin proteins by combined twodimensional gel electrophoresis and tandem mass spectrometry. Proteomics 5:2859-2865. (Pubitemid 41059763)
    • (2005) Proteomics , vol.5 , Issue.11 , pp. 2859-2865
    • Mamone, G.1    Addeo, F.2    Chianese, L.3    Di Luccia, A.4    De Martino, A.5    Nappo, A.6    Formisano, A.7    De Vivo, P.8    Ferranti, P.9
  • 199
    • 0034129841 scopus 로고    scopus 로고
    • Qualitative and quantitative analysis of wheat gluten proteins by liquid chromatography and electrospray mass spectrometry
    • Mamone, G., P. Ferranti, L. Chianese, L. Scafuri, and F. Addeo. 2000. Qualitative and quantitative analysis of wheat gluten proteins by liquid chromatography and electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 14:897-904. (Pubitemid 30367580)
    • (2000) Rapid Communications in Mass Spectrometry , vol.14 , Issue.10 , pp. 897-904
    • Mamone, G.1    Ferranti, P.2    Chianese, L.3    Scafuri, L.4    Addeo, F.5
  • 201
    • 74049126605 scopus 로고    scopus 로고
    • Analysis of food proteins and peptides by mass spectrometry-based techniques
    • Mamone, G., G. Picariello, S. Caira, F. Addeo, and P. Ferranti. 2009. Analysis of food proteins and peptides by mass spectrometry-based techniques. J. Chromatogr. A 1216:7130-7142.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 7130-7142
    • Mamone, G.1    Picariello, G.2    Caira, S.3    Addeo, F.4    Ferranti, P.5
  • 202
    • 0028202162 scopus 로고
    • Purification and characterization of three isolectins of soybean agglutinin. Evidence for C-terminal truncation by electrospray ionization mass spectrometry
    • Mandal, D. K., E. Nieves, L. Bhattacharyya, G. A. Orr, J. Roboz, Q. T. Yu, and C. F. Brewer. 1994. Purification and characterization of three isolectins of soybean agglutinin. Evidence for C-terminal truncation by electrospray ionization mass spectrometry. Eur. J. Biochem. 221:547-553. (Pubitemid 24120600)
    • (1994) European Journal of Biochemistry , vol.221 , Issue.1 , pp. 547-553
    • Mandal, D.K.1    Nieves, E.2    Bhattacharyya, L.3    Orr, G.A.4    Roboz, J.5    Yu, Q.6    Brewer, C.F.7
  • 203
    • 29544434691 scopus 로고    scopus 로고
    • Proteome modifications of blue mussel (Mytilus edulis L.) gills as an effect of water pollution
    • DOI 10.1002/pmic.200401328
    • Manduzio, H., P. Cosette, L. Gricourt, T. Jouenne, C. Lenz, O. K. Andersen, F. Leboulenger, and B. Rocher. 2005. Proteome modifications of blue mussel (Mytilus edulis L.) gills as an effect of water pollution. Proteomics 5:4958-4963. (Pubitemid 43016914)
    • (2005) Proteomics , vol.5 , Issue.18 , pp. 4958-4963
    • Manduzio, H.1    Cosette, P.2    Gricourt, L.3    Jouenne, T.4    Lenz, C.5    Andersen, O.-K.6    Leboulenger, F.7    Rocher, B.8
  • 204
    • 35348963096 scopus 로고    scopus 로고
    • The chicken egg white proteome
    • DOI 10.1002/pmic.200700397
    • Mann, K. 2007. The chicken egg white proteome. Proteomics 7: 3558-3568. (Pubitemid 47597677)
    • (2007) Proteomics , vol.7 , Issue.19 , pp. 3558-3568
    • Mann, K.1
  • 205
    • 46049101500 scopus 로고    scopus 로고
    • Proteomic analysis of the chicken egg vitelline membrane
    • DOI 10.1002/pmic.200800032
    • Mann, K. 2008. Proteomic analysis of the chicken egg vitelline membrane. Proteomics 8:2322-2332. (Pubitemid 351898036)
    • (2008) Proteomics , vol.8 , Issue.11 , pp. 2322-2332
    • Mann, K.1
  • 206
    • 33746001133 scopus 로고    scopus 로고
    • Proteomic analysis of the acid-soluble organic matrix of the chicken calcified eggshell layer
    • DOI 10.1002/pmic.200600120
    • Mann, K., B. Maček, and J. V. Olsen. 2006. Proteomic analysis of the acid-soluble organic matrix of the chicken calcified eggshell layer. Proteomics 6:3801-3810. (Pubitemid 44065158)
    • (2006) Proteomics , vol.6 , Issue.13 , pp. 3801-3810
    • Mann, K.1    Macek, B.2    Olsen, J.V.3
  • 207
    • 38149103492 scopus 로고    scopus 로고
    • The chicken egg yolk plasma and granule proteomes
    • Mann, K., and M. Mann. 2008. The chicken egg yolk plasma and granule proteomes. Proteomics 8:178-191.
    • (2008) Proteomics , vol.8 , pp. 178-191
    • Mann, K.1    Mann, M.2
  • 208
    • 45549093572 scopus 로고    scopus 로고
    • Identification of new chicken egg proteins by mass spectrometry-based proteomic analysis
    • DOI 10.1017/S0043933907001808, PII S0043933907001808
    • Mann, K., J. V. Olsen, B. Maček, F. Gnad, and M. Mann. 2008. Identification of new chicken egg proteins by mass spectrometry-based proteomic analysis. World's Poult. Sci. J. 64:209-218. (Pubitemid 351860426)
    • (2008) World's Poultry Science Journal , vol.64 , Issue.2 , pp. 209-218
    • Mann, K.1    Olsen, J.V.2    MacEk, B.3    Gnad, F.4    Mann, M.5
  • 209
    • 19744367828 scopus 로고    scopus 로고
    • Application of proteomics to the characterisation of milk and dairy products
    • Manso, M. A., J. Léonil, G. Jan, and V. Gagnaire. 2004. Application of proteomics to the characterisation of milk and dairy products. Int. Dairy J. 15:845-855.
    • (2004) Int. Dairy J. , vol.15 , pp. 845-855
    • Manso, M.A.1    Léonil, J.2    Jan, G.3    Gagnaire, V.4
  • 210
    • 0000216602 scopus 로고
    • Reversed-phase high-performance liquid chromatographic analysis of wheat proteins using a new, highly stable column
    • Marchylo, B. A., D. W. Hatcher, J. E. Kruger, and J. J. Kirkland. 1992. Reversed-phase high-performance liquid chromatographic analysis of wheat proteins using a new, highly stable column. Cereal Chem. 69:371-378.
    • (1992) Cereal Chem. , vol.69 , pp. 371-378
    • Marchylo, B.A.1    Hatcher, D.W.2    Kruger, J.E.3    Kirkland, J.J.4
  • 211
    • 0039073709 scopus 로고
    • Quantitative reverse-phase high-performance liquid chromatographic analysis of wheat storage proteins as a potential quality prediction tool
    • Marchylo, B. A., J. E. Kruger, and D. W. Hatcher. 1989. Quantitative reverse-phase high-performance liquid chromatographic analysis of wheat storage proteins as a potential quality prediction tool. J. Cereal Sci. 9:113-130.
    • (1989) J. Cereal Sci. , vol.9 , pp. 113-130
    • Marchylo, B.A.1    Kruger, J.E.2    Hatcher, D.W.3
  • 212
    • 0033790922 scopus 로고    scopus 로고
    • Characterization and sequence elucidation of a novel peptide with molt-inhibiting activity from the South African spiny lobster, Jasus lalandii
    • Marco, H. G., S. Stoeva, W. Voelter, and G. Gäde. 2000. Characterization and sequence elucidation of a novel peptide with molt-inhibiting activity from the South African spiny lobster, Jasus lalandii. Peptides 21:1313-1321.
    • (2000) Peptides , vol.21 , pp. 1313-1321
    • Marco, H.G.1    Stoeva, S.2    Voelter, W.3    Gäde, G.4
  • 213
    • 0031970418 scopus 로고    scopus 로고
    • Mass determination of low-molecular-weight proteins in phloem sap using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Marentes, E., and M. Grusak. 1998. Mass determination of lowmolecular-weight proteins in phloem sap using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Exp. Bot. 49:903-911. (Pubitemid 28226630)
    • (1998) Journal of Experimental Botany , vol.49 , Issue.322 , pp. 903-911
    • Marentes, E.1    Grusak, M.A.2
  • 214
    • 43949171177 scopus 로고
    • r subunits of glutenin by combined chromatographic (RP-HPLC) and electrophoretic separations and restriction fragment length polymorphism (RFLP) analyses of their encoding genes
    • r subunits of glutenin by combined chromatographic (RP-HPLC) and electrophoretic separations and restriction fragment length polymorphism (RFLP) analyses of their encoding genes. J. Cereal Sci. 17:221-236.
    • (1993) J. Cereal Sci. , vol.17 , pp. 221-236
    • Margiotta, B.1    Colaprico, G.2    D'Ovidio, R.3    Lafiandra, D.4
  • 217
    • 0035722641 scopus 로고    scopus 로고
    • Proteome analysis of rainbow trout (Oncorhynchus mykiss) liver proteins during short term starvation
    • DOI 10.1023/A:1014015530045
    • Martin, S. A. M., P. Cash, S. Blaney, and D. F. Houlihan. 2001. Proteome analysis of rainbow trout (Oncorhynchus mykiss) liver proteins during short term starvation. Fish Physiol. Biochem. 24: 259-270. (Pubitemid 34182970)
    • (2001) Fish Physiology and Biochemistry , vol.24 , Issue.3 , pp. 259-270
    • Martin, S.A.M.1    Cash, P.2    Blaney, S.3    Houlihan, D.F.4
  • 219
    • 60449099557 scopus 로고    scopus 로고
    • Differential protein expression in Corbicula fluminea upon exposure to a Microcystis aeruginosa toxic strain
    • Martins, J. C., P. N. Leão, and V. Vasconcelos. 2009. Differential protein expression in Corbicula fluminea upon exposure to a Microcystis aeruginosa toxic strain. Toxicon 53:409-416.
    • (2009) Toxicon , vol.53 , pp. 409-416
    • Martins, J.C.1    Leão, P.N.2    Vasconcelos, V.3
  • 220
    • 85006958730 scopus 로고
    • Characterization of low molecular weight glutenin subunits in durum wheat by reversed-phase high-performance liquid chromatography and N-terminal sequencing
    • Masci, S., E. J. L. Lew, D. Lafiandra, E. Porceddu, and D. D. Kasarda. 1995. Characterization of low molecular weight glutenin subunits in durum wheat by reversed-phase high-performance liquid chromatography and N-terminal sequencing. Cereal Chem. 72:100-104.
    • (1995) Cereal Chem. , vol.72 , pp. 100-104
    • Masci, S.1    Lew, E.J.L.2    Lafiandra, D.3    Porceddu, E.4    Kasarda, D.D.5
  • 222
    • 0033008698 scopus 로고    scopus 로고
    • Analysis of polyphenols using capillary zone electrophoresis and HPLC: Detection of soy, lupin, and pea protein in meat products
    • DOI 10.1021/jf980749h
    • Mellenthin, O., and R. Galensa. 1999. Analysis of polyphenols using capillary zone electrophoresis and HPLC: detection of soy, lupin, and pea protein in meat products. J. Agric. Food Chem. 47: 594-602. (Pubitemid 29185230)
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.2 , pp. 594-602
    • Mellenthin, O.1    Galensa, R.2
  • 223
    • 0028011430 scopus 로고
    • The seed storage proteins from Lupinus albus
    • DOI 10.1016/S0031-9422(00)90331-5
    • Melo, T. S., R. B. Ferreira, and A. N. Teixeira. 1994. The seed storage proteins from Lupinus albus. Phytochemistry 37:641-648 (Pubitemid 2156034)
    • (1994) Phytochemistry , vol.37 , Issue.3 , pp. 641-648
    • Melo, T.S.1    Ferreira, R.B.2    Teixeira, A.N.3
  • 224
  • 226
    • 0001576715 scopus 로고
    • Molecular and spectroscopic characterisation of a low molecular weight seed storage protein from yellow mustard (Sinapis alba L.)
    • Menéndez-Arias, L., R. I. Monsalve, J. G. Gavilanes, and R. Rodríguez. 1987. Molecular and spectroscopic characterisation of a low molecular weight seed storage protein from yellow mustard (Sinapis alba L.). Int. J. Biochem. 19:899-907.
    • (1987) Int. J. Biochem. , vol.19 , pp. 899-907
    • Menéndez-Arias, L.1    Monsalve, R.I.2    Gavilanes, J.G.3    Rodríguez, R.4
  • 228
    • 34147139944 scopus 로고    scopus 로고
    • Peroxisomal proteomic approach for protein profiling in blue mussels (Mytilus edulis) exposed to crude oil
    • DOI 10.1080/13547500600943528, PII 768587648
    • Mi, J., I. Apraiz, and S. Cristóbal. 2007. Peroxisomal proteomic approach for protein profiling in blue mussels (Mytilus edulis) exposed to crude oil. Biomarkers 12:47-60. (Pubitemid 46562625)
    • (2007) Biomarkers , vol.12 , Issue.1 , pp. 47-60
    • Mi, J.1    Apraiz, I.2    Cristobal, S.3
  • 229
    • 27144530363 scopus 로고    scopus 로고
    • Peroxisomal proteomics, a new tool for risk assessment of peroxisome proliferating pollutants in the marine environment
    • DOI 10.1002/pmic.200401243
    • Mi, J., A. Orbea, N. Syme, M. Ahmed, M. P. Cajaraville, and S. Cristóbal. 2005. Peroxisomal proteomics, a new tool for risk assessment of peroxisome proliferating pollutants in the marine environment. Proteomics 5:3954-3965. (Pubitemid 41502491)
    • (2005) Proteomics , vol.5 , Issue.15 , pp. 3954-3965
    • Mi, J.1    Orbea, A.2    Syme, N.3    Ahmed, M.4    Cajaraville, M.P.5    Cristobal, S.6
  • 230
    • 0030606856 scopus 로고    scopus 로고
    • Reversed-phase high-performance liquid chromatographic separation of bovine κ-casein macropeptide and characterization of isolated fractions
    • DOI 10.1016/0021-9673(96)00122-7
    • Minikiewicz, P., C. J. Slangen, F. M. Lagerwerf, J. Haverkamp, H. S. Rollema, and S. Visser. 1996. Reversed-phase high-performance liquid chromatographic separation of bovine k-casein macropeptide and characterization of isolated fractions. J. Chromatogr. A 743: 123-135. (Pubitemid 26316387)
    • (1996) Journal of Chromatography A , vol.743 , Issue.1 , pp. 123-135
    • Minkiewicz, P.1    Slangen, C.J.2    Lagerwerf, F.M.3    Haverkamp, J.4    Rollema, H.S.5    Visser, S.6
  • 231
    • 1542609972 scopus 로고    scopus 로고
    • Mass mapping analysis as a tool for the identification of genetic variants of bovine β-casein
    • DOI 10.1016/S0021-9673(03)00955-5, PII S0021967303009555
    • Miralles, B., J. Leaver, M. Ramos, and L. Amigo. 2003. Mass mapping analysis as a tool for the identification of genetic variants of bovine b-casein. J. Chromatogr. A 1007:47-53. (Pubitemid 38352600)
    • (2003) Journal of Chromatography A , vol.1007 , Issue.1-2 , pp. 47-53
    • Miralles, B.1    Leaver, J.2    Ramos, M.3    Amigo, L.4
  • 232
    • 13844315284 scopus 로고    scopus 로고
    • Nanoflow liquid chromatography coupled to matrix-assisted laser desorption/ionization mass spectrometry: Sample preparation, data analysis, and application to the analysis of complex peptide mixtures
    • DOI 10.1002/pmic.200400984
    • Mirgorodskaya, E., C. Braeuer, P. Fucini, H. Lehrach, and J. Gobom. 2005. Nanoflow liquid chromatography coupled to matrixassisted laser desorption/ionization mass spectrometry: sample preparation, data analysis, and application to the analysis of complex peptide mixtures. Proteomics 5:399-408. (Pubitemid 40262056)
    • (2005) Proteomics , vol.5 , Issue.2 , pp. 399-408
    • Mirgorodskaya, E.1    Braeuer, C.2    Fucini, P.3    Lehrach, H.4    Gobom, J.5
  • 233
    • 0034623394 scopus 로고    scopus 로고
    • Approaches towards the quantitative analysis of peptides and proteins by reversed-phase high-performance liquid chromatography in the absence of a pure reference sample
    • Moffatt, F., P. Senkans, and D. Ricketts. 2000. Approaches towards the quantitative analysis of peptides and proteins by reversed-phase high-performance liquid chromatography in the absence of a pure reference sample. J. Chromatogr. A 891:235-242.
    • (2000) J. Chromatogr. A , vol.891 , pp. 235-242
    • Moffatt, F.1    Senkans, P.2    Ricketts, D.3
  • 234
    • 60649112096 scopus 로고    scopus 로고
    • Comparison of electrospray and matrix-assisted laser desorption ionization on the same hybrid quadrupole time-of-flight tandem mass spectrometer: Application to bidimensional liquid chromatography of proteins from bovine milk fraction
    • Mollé, D., J. Jardin, M. Piot, M. Pasco, J. Léonil, and V. Gagnaire. 2009. Comparison of electrospray and matrix-assisted laser desorption ionization on the same hybrid quadrupole time-of-flight tandem mass spectrometer: application to bidimensional liquid chromatography of proteins from bovine milk fraction. J. Chromatogr. A 1216:2424-2432.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 2424-2432
    • Mollé, D.1    Jardin, J.2    Piot, M.3    Pasco, M.4    Léonil, J.5    Gagnaire, V.6
  • 235
    • 0028984229 scopus 로고
    • Heterogeneity of the bovine k-casein caseinomacropeptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry
    • Mollé, D., and J. Léonil. 1995. Heterogeneity of the bovine k-casein caseinomacropeptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry. J. Chromatogr. A 708:223-230.
    • (1995) J. Chromatogr. A , vol.708 , pp. 223-230
    • Mollé, D.1    Léonil, J.2
  • 236
    • 16244387942 scopus 로고    scopus 로고
    • Quantitative determination of bovine κ-casein macropeptide in dairy products by Liquid chromatography/Electrospray coupled to mass spectrometry (LC-ESI/MS) and Liquid chromatography/Electrospray coupled to tamdem mass spectrometry (LC-ESI/MS/MS)
    • DOI 10.1016/j.idairyj.2004.08.013
    • Mollé, D., and J. Léonil. 2005. Quantitative determination of bovine k-casein macropeptide in dairy products by liquid chromatography/ electrospray coupled to mass spectrometry (LC-ESI/MS) and liquid chromatography/electrospray coupled to tandem mass spectrometry (LC-ESI/MS/MS). Int. Dairy J. 15:419-428. (Pubitemid 40451653)
    • (2005) International Dairy Journal , vol.15 , Issue.5 , pp. 419-428
    • Molle, D.1    Leonil, J.2
  • 237
    • 0032524087 scopus 로고    scopus 로고
    • Selective detection of lactolated peptides in hydrolysates by liquid chromatography/electrospray tandem mass spectrometry
    • DOI 10.1006/abio.1998.2636
    • Mollé, D., F. Morgan, S. Bouhallab, and J. Léonil. 1998. Selective detection of lactolated peptides in hydrolysates by liquid chromatography/ electrospray tandem mass spectrometry. Anal. Biochem. 259:152-161. (Pubitemid 28247063)
    • (1998) Analytical Biochemistry , vol.259 , Issue.1 , pp. 152-161
    • Molle, D.1    Morgan, F.2    Bouhallab, S.3    Leonil, J.4
  • 238
    • 34247643756 scopus 로고    scopus 로고
    • Effect of heat treatment on the detection of intact bovine β-lactoglobulins by LC mass spectrometry
    • DOI 10.1021/jf063083x
    • Monaci, L., and A. J. van Hengel. 2007. Effect of heat treatment on the detection of intact bovine β-lactoglobulins by LC mass spectrometry. J. Agric. Food Chem. 55:2985-2992. (Pubitemid 46668308)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.8 , pp. 2985-2992
    • Monaci, L.1    Van Hengel, A.J.2
  • 239
    • 42649101981 scopus 로고    scopus 로고
    • Development of a method for the quantification of whey allergen traces in mixed-fruit juices based on liquid chromatography with mass spectrometric detection
    • Monaci, L., and A. J. van Hengel. 2008. Development of a method for the quantification of whey allergen traces in mixed-fruit juices based on liquid chromatography with mass spectrometric detection. J. Chromatogr. A 1192:113-120.
    • (2008) J. Chromatogr. A , vol.1192 , pp. 113-120
    • Monaci, L.1    Van Hengel, A.J.2
  • 240
    • 67349171915 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics methods for analysis of food allergens
    • Monaci, L., and A. Visconti. 2009. Mass spectrometry-based proteomics methods for analysis of food allergens. Trends Anal. Chem. 28:581-591.
    • (2009) Trends Anal. Chem. , vol.28 , pp. 581-591
    • Monaci, L.1    Visconti, A.2
  • 242
    • 33749526135 scopus 로고    scopus 로고
    • Data processing and classification analysis of proteomic changes: A case study of oil pollution in the mussel, Mytilus edulis
    • Monsinjon, T., O. K. Andersen, F. Leboulenger, and T. Knigge. 2006. Data processing and classification analysis of proteomic changes: a case study of oil pollution in the mussel, Mytilus edulis. Proteome Sci. 4:17-30.
    • (2006) Proteome Sci. , vol.4 , pp. 17-30
    • Monsinjon, T.1    Andersen, O.K.2    Leboulenger, F.3    Knigge, T.4
  • 243
    • 3242774747 scopus 로고    scopus 로고
    • High-throughput peptide mass fingerprinting of soybean seed proteins: Automated workflow and utility of UniGene expressed sequence tag databases for protein identification
    • DOI 10.1016/j.phytochem.2004.04.011, PII S0031942204001621
    • Mooney, B. P., H. B. Krishnan, and J. J. Thelen. 2004. Highthroughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification. Phytochemistry 65:1733-1744. (Pubitemid 38969919)
    • (2004) Phytochemistry , vol.65 , Issue.12 , pp. 1733-1744
    • Mooney, B.P.1    Thelen, J.J.2
  • 245
    • 0037189870 scopus 로고    scopus 로고
    • Characterization and functional properties of lactosyl caseinomacropeptide conjugates
    • DOI 10.1021/jf020118u
    • Moreno, F. J., R. López-Fandiñ o, and A. Olano. 2002. Characterization and functional properties of lactosyl caseinomacropeptide conjugates. J. Agric. Food Chem. 50:5179-5184. (Pubitemid 34925109)
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.18 , pp. 5179-5184
    • Moreno, F.J.1    Lopez-Fandino, R.2    Olano, A.3
  • 246
    • 25144519047 scopus 로고    scopus 로고
    • Thermostability and in vitro digestibility of a purified major allergen 2S albumin (Ses i 1) from white sesame seeds (Sesamum indicum L.)
    • DOI 10.1016/j.bbapap.2005.07.022, PII S1570963905002529
    • Moreno, F. J., B. M. Maldonado, N. Wellner, and E. N. Mills. 2005. Thermostability and in vitro digestibility of a purified major allergen 2S albumin (Ses i 1) from white sesame seeds (Sesamum indicum L.). Biochim. Biophys. Acta 1752:142-153. (Pubitemid 41338062)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1752 , Issue.2 , pp. 142-153
    • Moreno, F.J.1    Maldonado, B.M.2    Wellner, N.3    Mills, E.N.C.4
  • 247
    • 0033826680 scopus 로고    scopus 로고
    • Chromatographic characterization of ovine kappa-casein macropeptide
    • Moreno, F. J., I. Recio, A. Olano, and R. López-Fandiñ o. 2000. Chromatographic characterization of ovine kappa-casein macropeptide. J. Dairy Res. 67:349-359.
    • (2000) J. Dairy Res. , vol.67 , pp. 349-359
    • Moreno, F.J.1    Recio, I.2    Olano, A.3    López-Fandiño, R.4
  • 249
    • 0030151307 scopus 로고    scopus 로고
    • Purification, characterization, and crystallization of single molecular species of β-conglycinin from soybean seeds
    • Morita, S., M. Fukase, M. Yamaguchi, Y. Fukuda, and Y. Morita. 1996. Purification, characterization, and crystallization of single molecular species of beta-conglycinin from soybean seeds. Biosci. Biotechnol. Biochem. 60:866-873. (Pubitemid 26311279)
    • (1996) Bioscience, Biotechnology and Biochemistry , vol.60 , Issue.5 , pp. 866-873
    • Morita, S.1    Fukase, M.2    Yamaguchi, M.3    Fukuda, Y.4    Morita, Y.5
  • 250
    • 0028180250 scopus 로고
    • Identification of proteins in polyacrylamide gels by mass spectrometric peptide mapping combined with database search
    • Mørtz, E., O. Vorm, M. Mann, and P. Roepstorff. 1994. Identification of proteins in polyacrylamide gels by mass spectrometric peptide mapping combined with database search. Biol. Mass Spectrom. 23:249-261.
    • (1994) Biol. Mass Spectrom. , vol.23 , pp. 249-261
    • Mørtz, E.1    Vorm, O.2    Mann, M.3    Roepstorff, P.4
  • 251
    • 0028821266 scopus 로고
    • Purification of allergenic proteins from peanut for preparation of the reactive solid phase of a specific IgE radioimmunoassay
    • Moutete, H. F., A. Olszewski, I. Gastin, F. Namour, D. A. Moneret-Vautrin, and J. L. Guéant. 1995. Purification of allergenic proteins from peanut for preparation of the reactive solid phase of a specific IgE radioimmunoassay. J. Chromatogr. B 664:211-217.
    • (1995) J. Chromatogr. B , vol.664 , pp. 211-217
    • Moutete, H.F.1    Olszewski, A.2    Gastin, I.3    Namour, F.4    Moneret-Vautrin, D.A.5    Guéant, J.L.6
  • 252
    • 14644397227 scopus 로고    scopus 로고
    • Characterization of B- and C-type low molecular weight glutenin subunits by electrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry
    • DOI 10.1002/pmic.200401029
    • Muccilli, V., V. Cunsolo, R. Saletti, S. Foti, S. Masci, and D. Lafiandra. 2005. Characterization of B-and C-type low molecular weight glutenin subunits by electrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry. Proteomics 5:719-728. (Pubitemid 40316056)
    • (2005) Proteomics , vol.5 , Issue.3 , pp. 719-728
    • Muccilli, V.1    Cunsolo, V.2    Saletti, R.3    Foti, S.4    Masci, S.5    Lafiandra, D.6
  • 254
    • 0031881985 scopus 로고    scopus 로고
    • Cloning of tropomyosins from lobster (Homarus americanus) striated muscles: Fast and slow isoforms may be generated from the same transcript
    • DOI 10.1023/A:1005352410725
    • Mykles, D. L., J. L. Cotton, H. Taniguchi, K. Sano, and Y. Maeda. 1998. Cloning of tropomyosins from lobster (Homarus americanus) striated muscles: fast and slow isoforms may be generated from the same transcript. J. Muscle Res. Cell Motil. 19:105-115. (Pubitemid 28126199)
    • (1998) Journal of Muscle Research and Cell Motility , vol.19 , Issue.2 , pp. 105-115
    • Mykles, D.L.1    Cotton, J.L.S.2    Taniguchi, H.3    Sano, K.-I.4    Maeda, Y.5
  • 256
    • 21244455506 scopus 로고    scopus 로고
    • Comparison of protein solubilization methods suitable for proteomic analysis of soybean seed proteins
    • DOI 10.1016/j.ab.2005.04.046, PII S0003269705003593
    • Natarajan, S., C. Xu, T. J. Caperna, and W. M. Garrett. 2005. Comparison of protein solubilization methods suitable for proteomic analysis of soybean seed proteins. Anal. Biochem. 342: 214-220. (Pubitemid 40884569)
    • (2005) Analytical Biochemistry , vol.342 , Issue.2 , pp. 214-220
    • Natarajan, S.1    Xu, C.2    Caperna, T.J.3    Garrett, W.M.4
  • 257
    • 69949097289 scopus 로고    scopus 로고
    • An efficient extraction method to enhance analysis of low abundant proteins from soybean seed
    • Natarajan, S. S., H. B. Krishnan, S. Lakshman, and W. M. Garrett. 2009. An efficient extraction method to enhance analysis of low abundant proteins from soybean seed. Anal. Biochem. 394:259-268.
    • (2009) Anal. Biochem. , vol.394 , pp. 259-268
    • Natarajan, S.S.1    Krishnan, H.B.2    Lakshman, S.3    Garrett, W.M.4
  • 258
    • 33646495734 scopus 로고    scopus 로고
    • Characterization of storage proteins in wild (Glycine boja) and cultivated (Glycine max) soybean seeds using proteomic analysis
    • Natarajan, S. S., C. Xu, H. Bae, T. J. Caperna, and W. M. Garrett. 2006. Characterization of storage proteins in wild (Glycine boja) and cultivated (Glycine max) soybean seeds using proteomic analysis. J. Agric. Food Chem. 54:3114-3120.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 3114-3120
    • Natarajan, S.S.1    Xu, C.2    Bae, H.3    Caperna, T.J.4    Garrett, W.M.5
  • 260
    • 43949166278 scopus 로고
    • Electrospray ionization mass spectrometry of phosphopeptides isolated by on-line immobi-lized metal-ion affinity chromatography
    • Nuwaysir, L. M., and J. T. Stults. 1993. Electrospray ionization mass spectrometry of phosphopeptides isolated by on-line immobi-lized metal-ion affinity chromatography. J. Am. Soc. Mass Spectrom. 4:662-669.
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 662-669
    • Nuwaysir, L.M.1    Stults, J.T.2
  • 262
    • 77953479720 scopus 로고    scopus 로고
    • Co-extraction of egg white proteins using ion-exchange chromatography from ovomucinremoved egg whites
    • doi:10.1016/j.jchromb. 2010.04.037
    • Omana, D. A., J. Wang, and J. Wu. 2010. Co-extraction of egg white proteins using ion-exchange chromatography from ovomucinremoved egg whites. J. Chromatogr. B. doi:10.1016/j.jchromb. 2010.04.037.
    • (2010) J. Chromatogr. B.
    • Omana, D.A.1    Wang, J.2    Wu, J.3
  • 264
    • 77649266589 scopus 로고    scopus 로고
    • Closely related shrimp species identification by MALDI-ToF mass spectrometry
    • Ortea, I., L. Barros, and J. M. Gallardo. 2009. Closely related shrimp species identification by MALDI-ToF mass spectrometry. J. Aquat. Food Prod. Technol. 18:146-155.
    • (2009) J. Aquat. Food Prod. Technol. , vol.18 , pp. 146-155
    • Ortea, I.1    Barros, L.2    Gallardo, J.M.3
  • 265
    • 67649875884 scopus 로고    scopus 로고
    • Arginine kinase peptide mass fingerprinting as a proteomic approach for species identification and taxonomic analysis of commercially relevant shrimp species
    • Ortea, I., B. Cañ as, P. Calo-Mata, J. Barros-Velázquez, and J. M. Gallardo. 2009. Arginine kinase peptide mass fingerprinting as a proteomic approach for species identification and taxonomic analysis of commercially relevant shrimp species. J. Agric. Food Chem. 57:5665-5672.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 5665-5672
    • Ortea, I.1    Cañas, B.2    Calo-Mata, P.3    Barros-Velázquez, J.4    Gallardo, J.M.5
  • 266
    • 70449336603 scopus 로고    scopus 로고
    • Mass spectrometry characterization of species-specific peptides from arginine kinase for the identification of commercially relevant shrimp species
    • Ortea, I., B. Cañ as, and J. M. Gallardo. 2009. Mass spectrometry characterization of species-specific peptides from arginine kinase for the identification of commercially relevant shrimp species. J. Proteome Res. 8:5356-5362.
    • (2009) J. Proteome Res. , vol.8 , pp. 5356-5362
    • Ortea, I.1    Cañas, B.2    Gallardo, J.M.3
  • 267
    • 0002561544 scopus 로고
    • Liquid chromatographic identification of common fish species
    • Osman, M. A., S. H. Ashoor, and P. C. Marsh. 1987. Liquid chromatographic identification of common fish species. J. AOAC Int. 70:618-625.
    • (1987) J. AOAC Int. , vol.70 , pp. 618-625
    • Osman, M.A.1    Ashoor, S.H.2    Marsh, P.C.3
  • 269
    • 34247516578 scopus 로고    scopus 로고
    • Cloning, sequencing, and recombinant production of Sin a 2, an allergenic 11S globulin from yellow mustard seeds
    • DOI 10.1016/j.jaci.2007.01.027, PII S0091674907002370
    • Palomares, O., A. Vereda, J. Cuesta-Herranz, M. Villalba, and R. Rodríguez. 2007. Cloning, sequencing, and recombinant production of Sin a 2, an allergenic 11S globulin from yellow mustard seeds. J. Allergy Clin. Immunol. 119:1189-1196. (Pubitemid 46654174)
    • (2007) Journal of Allergy and Clinical Immunology , vol.119 , Issue.5 , pp. 1189-1196
    • Palomares, O.1    Vereda, A.2    Cuesta-Herranz, J.3    Villalba, M.4    Rodriguez, R.5
  • 271
    • 0031014216 scopus 로고    scopus 로고
    • Primary structure and allergenic activity of trypsin inhibitors from the seeds of buckwheat (Fagopyrum esculentum Moench)
    • DOI 10.1016/S0014-5793(96)01367-1, PII S0014579396013671
    • Park, S. S., K. Abe, M. Kimura, A. Urisu, and N. Yamasaki. 1997. Primary structure and allergenic activity of trypsin inhibitors from the seeds of
    • (1997) FEBS Letters , vol.400 , Issue.1 , pp. 103-107
    • Park, S.-S.1    Abe, K.2    Kimura, M.3    Urisu, A.4    Yamasaki, N.5
  • 275
    • 0001906328 scopus 로고
    • Subunit composition of wheat glutenin protein, isolated by gel filtration in a dissociating medium
    • Payne, P. I., and K. G. Corfield. 1979. Subunit composition of wheat glutenin protein, isolated by gel filtration in a dissociating medium. Planta 145:83-88.
    • (1979) Planta , vol.145 , pp. 83-88
    • Payne, P.I.1    Corfield, K.G.2
  • 277
    • 0000408625 scopus 로고
    • Scale-up from analytical to preparative reversed-phase high-performance liquid chromatography of soybean glycinin
    • Peterson, R. E., and W. J. Wolf. 1988. Scale-up from analytical to preparative reversed-phase high-performance liquid chromatography of soybean glycinin. J. Chromatogr. A 444:263-268.
    • (1988) J. Chromatogr. A , vol.444 , pp. 263-268
    • Peterson, R.E.1    Wolf, W.J.2
  • 278
    • 0000317295 scopus 로고
    • Enhancement of highperformance liquid chromatography of soybean proteins by addition of sodium dodecyl sulfate
    • Peterson, R. E., and W. J. Wolf. 1992. Enhancement of highperformance liquid chromatography of soybean proteins by addition of sodium dodecyl sulfate. Cereal Chem. 69:101-102.
    • (1992) Cereal Chem. , vol.69 , pp. 101-102
    • Peterson, R.E.1    Wolf, W.J.2
  • 280
    • 77956442721 scopus 로고    scopus 로고
    • The role of proteomics in the study of the influence of climate change on seafood products
    • doi:10.1016/j.foodres.2009. 11.012
    • Piñeiro, C., B. Cañ as, and M. Carrera. 2010. The role of proteomics in the study of the influence of climate change on seafood products. Food Res. Int. 43:1791-1802. doi:10.1016/j.foodres.2009. 11.012.
    • (2010) Food Res. Int. , vol.43 , pp. 1791-1802
    • Piñeiro, C.1    Cañas, B.2    Carrera, M.3
  • 282
    • 0342538903 scopus 로고    scopus 로고
    • Characterization and partial sequencing of species-specific sarcoplasmic polypeptides from commercial hake species by mass spectrometry following two-dimensional electrophoresis
    • DOI 10.1002/1522-2683(200105)22:8<1545::AID-ELPS1545>3.0.CO;2-5
    • Piñeiro, C., J. Vázquez, A. I. Marina, J. Barros-Velázquez, and J. M. Gallardo. 2001. Characterization and partial sequencing of speciesspecific sarcoplasmic polypeptides from commercial hake species by mass spectrometry following two-dimensional electrophoresis. Electrophoresis 22:1545-1552. (Pubitemid 32452102)
    • (2001) Electrophoresis , vol.22 , Issue.8 , pp. 1545-1552
    • Pineiro, C.1    Vazquez, J.2    Marina, A.I.3    Barros-Velezquez, J.4    Gallardo, J.M.5
  • 283
    • 1142287446 scopus 로고    scopus 로고
    • Methods for allergen analysis in food: A review
    • DOI 10.1080/02652030310001620423
    • Poms, R. E., C. L. Klein, and E. Anklam. 2004. Methods for allergen analysis in food: a review. Food Addit. Contam. 21:1-31. (Pubitemid 38208313)
    • (2004) Food Additives and Contaminants , vol.21 , Issue.1 , pp. 1-31
    • Poms, R.E.1    Klein, C.L.2    Anklam, E.3
  • 285
    • 53149140998 scopus 로고    scopus 로고
    • Characterization of wheat gluten proteins by HPLC and MALDI TOF mass spectrometry
    • Qian, Y., K. Preston, O. Krokhin, J. Mellish, and W. Ens. 2008. Characterization of wheat gluten proteins by HPLC and MALDI TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 19:1542-1550.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1542-1550
    • Qian, Y.1    Preston, K.2    Krokhin, O.3    Mellish, J.4    Ens, W.5
  • 286
    • 77953128629 scopus 로고    scopus 로고
    • Iron stabilizes thylakoid protein-pigment complexes in Indian mustard during Cd-phytoremediation as revealed by BNSDS-PAGE and ESI-MS/MS
    • Qureshi, M. I., G. M. D'Amici, M. Fagioni, S. Rinalducci, and L. Zolla. 2010. Iron stabilizes thylakoid protein-pigment complexes in Indian mustard during Cd-phytoremediation as revealed by BNSDS-PAGE and ESI-MS/MS. J. Plant Physiol. 167:761-770.
    • (2010) J. Plant Physiol. , vol.167 , pp. 761-770
    • Qureshi, M.I.1    D'Amici, G.M.2    Fagioni, M.3    Rinalducci, S.4    Zolla, L.5
  • 287
    • 0001747195 scopus 로고
    • Isolation and characterization of b-globulin low molecular weight protein fraction from sesame seed (Sesamum indicum L.)
    • Rajendran, S., and V. Prakash. 1988. Isolation and characterization of b-globulin low molecular weight protein fraction from sesame seed (Sesamum indicum L.). J. Agric. Food Chem. 36:269-275.
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 269-275
    • Rajendran, S.1    Prakash, V.2
  • 288
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • DOI 10.1038/nprot.2007.261, PII NPROT.2007.261
    • Rappsilber, J., M. Mann, and Y. Ishihama. 2007. Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2:1896-1906. (Pubitemid 47308128)
    • (2007) Nature Protocols , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 289
    • 29344464592 scopus 로고    scopus 로고
    • Surface enhanced laser desorptions ionization-time of flight-mass spectrometry analysis in complex food and biological systems
    • DOI 10.1002/mnfr.200500047
    • Rawel, H. M., S. Rohn, J. Kroll, and F. J. Schweigert. 2005. Surface enhanced laser desorptions ionization-time of flight-mass spectrometry analysis in complex food and biological systems. Mol. Nutr. Food Res. 49:1104-1111. (Pubitemid 43004342)
    • (2005) Molecular Nutrition and Food Research , vol.49 , Issue.12 , pp. 1104-1111
    • Rawel, H.M.1    Rohn, S.2    Kroll, J.3    Schweigert, F.J.4
  • 290
    • 0000419526 scopus 로고    scopus 로고
    • Protein Changes in Stored Ultra-High-Temperature-Treated Milks Studied by Capillary Electrophoresis and High-Performance Liquid Chromatography
    • Recio, I., M. de Frutos, A. Olano, and M. Ramos. 1996. Protein changes in stored ultra-high-temperature-treated milks studied by capillary electrophoresis and high-performance liquid chromatography. J. Agric. Food Chem. 44:3955-3959. (Pubitemid 126453400)
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , Issue.12 , pp. 3955-3959
    • Recio, I.1    De Frutos, M.2    Olano, A.3    Ramos, M.4
  • 291
    • 67249143460 scopus 로고    scopus 로고
    • Composition, vigor, and proteome of mature soybean seeds developed under high temperature
    • Ren, C., K. D. Bilyeu, and P. R. Beuselinck. 2009. Composition, vigor, and proteome of mature soybean seeds developed under high temperature. Crop Sci. 49:1010-1022.
    • (2009) Crop Sci. , vol.49 , pp. 1010-1022
    • Ren, C.1    Bilyeu, K.D.2    Beuselinck, P.R.3
  • 294
    • 0028985359 scopus 로고
    • Characterization of distinct alpha-and gamma-type gliadins and low molecular weight components from wheat endosperm as coeliac immunoreactive proteins
    • Rocher, A., F. Soriano, E. Molina, G. González-Limas, and E. Méndez. 1995. Characterization of distinct alpha-and gamma-type gliadins and low molecular weight components from wheat endosperm as coeliac immunoreactive proteins. Biochim. Biophys. Acta 1247:143-148.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 143-148
    • Rocher, A.1    Soriano, F.2    Molina, E.3    González-Limas, G.4    Méndez, E.5
  • 295
    • 0042861622 scopus 로고    scopus 로고
    • Changes in protein expression profiles in bivalve molluscs (Chamaelea gallina) exposed to four model environmental pollutants
    • DOI 10.1002/pmic.200300491
    • Rodríguez-Ortega, M. J., B. E. Grøsvik, A. Rodríguez-Ariza, A. Goksøyr, and J. López-Barea. 2003. Changes in protein expression profiles in bivalve molluscs (Chamalea gallina) exposed to four model environmental pollutants. Proteomics 3:1535-1543. (Pubitemid 37048079)
    • (2003) Proteomics , vol.3 , Issue.8 , pp. 1535-1543
    • Rodriguez-Ortega, M.J.1    Grosvik, B.E.2    Rodriguez-Ariza, A.3    Goksoyr, A.4    Lopez-Barea, J.5
  • 299
    • 0032765879 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry in evaluation of protein profiles of infant formulae
    • Sabbadin, S., R. Seraglia, G. Allegri, A. Bertazzo, and P. Traldi. 1999. Matrix-assisted laser desorption/ionization mass spectrometry in evaluation of protein profiles of infant formulae. Rapid Commun. Mass Spectrom. 13:1438-1443. (Pubitemid 29345293)
    • (1999) Rapid Communications in Mass Spectrometry , vol.13 , Issue.14 , pp. 1438-1443
    • Sabbadin, S.1    Seraglia, R.2    Allegri, G.3    Bertazzo, A.4    Traldi, P.5
  • 302
    • 17144368764 scopus 로고    scopus 로고
    • Identification and quantification of ε-(γ-glutamyl)lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS)
    • Schäfer, C., M. Schott, F. Brandl, S. Neidhart, and R. Carle. 2005. Identification and quantification of ε-(γ-glutamyl)lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS). J. Agric. Food Chem. 20:2830-2837. (Pubitemid 40525240)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.8 , pp. 2830-2837
    • Schafer, C.1    Schott, M.2    Brandl, F.3    Neidhart, S.4    Carle, R.5
  • 303
    • 0031841153 scopus 로고    scopus 로고
    • Peptide mass fingerprint sequence coverage from differently stained proteins on two-dimensional electrophoresis patterns by matrix assisted laser desorption/ionization-mass spectrometry (MALDI-MS)
    • DOI 10.1002/elps.1150190607
    • Scheler, C., S. Lamer, Z. Pan, X. P. Li, J. Salnikow, and P. Jungblut. 1999. Peptide mass fingerprint sequence coverage from differently stained proteins on two-dimensional electrophoresis patterns by matrix assisted laser desorption/ionization-mass spectrometry (MALDI-MS). Electrophoresis 19:918-927. (Pubitemid 28239961)
    • (1998) Electrophoresis , vol.19 , Issue.6 , pp. 918-927
    • Scheler, C.1    Lamer, S.2    Pan, Z.3    Li, X.-P.4    Salnikow, J.5    Jungblut, P.6
  • 304
    • 49249092611 scopus 로고    scopus 로고
    • Identification by proteome analysis of muscle proteins in sea bream (Sparus aurata)
    • Schiavone, R., L. Zilli, C. Storelli, and S. Vilella. 2008. Identification by proteome analysis of muscle proteins in sea bream (Sparus aurata). J. Eur. Food Res. Technol. 227:1403-1410.
    • (2008) J. Eur. Food Res. Technol. , vol.227 , pp. 1403-1410
    • Schiavone, R.1    Zilli, L.2    Storelli, C.3    Vilella, S.4
  • 306
    • 77952999879 scopus 로고    scopus 로고
    • Analysis of oligomeric protein complexes in the chloroplast subproteome of nucleic acid-binding proteins from mustard reveals potential redox regulators of plastid gene expression
    • Schröter, Y., S. Steiner, K. Matthäi, and T. Pfannschmidt. 2010. Analysis of oligomeric protein complexes in the chloroplast subproteome of nucleic acid-binding proteins from mustard reveals potential redox regulators of plastid gene expression. Proteomics 10: 1-14.
    • (2010) Proteomics , vol.10 , pp. 1-14
    • Schröter, Y.1    Steiner, S.2    Matthäi, K.3    Pfannschmidt, T.4
  • 307
    • 0042634234 scopus 로고    scopus 로고
    • Analysis of proteins in the spent culture medium of Lupinus albus by electrospray ionisation tandem mass spectrometry
    • DOI 10.1016/S0021-9673(03)00622-8
    • Schwend, T., I. Redwanz, T. Ruppert, A. Szenthe, and M. Wink. 2003. Analysis of proteins in the spent culture medium of Lupinus albus by electrospray ionisation tandem mass spectrometry. J. Chromatogr. A 1009:105-110. (Pubitemid 36966674)
    • (2003) Journal of Chromatography A , vol.1009 , Issue.1-2 , pp. 105-110
    • Schwend, T.1    Redwanz, I.2    Ruppert, T.3    Szenthe, A.4    Wink, M.5
  • 308
    • 33750319346 scopus 로고    scopus 로고
    • Orbitrap mass analyzer - Overview and applications in proteomics
    • DOI 10.1002/pmic.200600528
    • Scigelova, M., and A. Makarov. 2006. Orbitrap mass analyzer-overview and applications in proteomics. Proteomics 6(Suppl. 2): 16-21. (Pubitemid 44625764)
    • (2006) Proteomics , vol.1 , Issue.1-2 SUPPL. , pp. 16-21
    • Scigelova, M.1    Makarov, A.2
  • 309
    • 77957076445 scopus 로고    scopus 로고
    • Oxidative stress and bivalves: A proteomic approach
    • Sheehan, D., and B. McDonagh. 2008. Oxidative stress and bivalves: a proteomic approach. Invert. Survival J. 5:110-123.
    • (2008) Invert. Survival J. , vol.5 , pp. 110-123
    • Sheehan, D.1    McDonagh, B.2
  • 310
    • 33751224458 scopus 로고    scopus 로고
    • Confirmation of peanut protein using peptide markers in dark chocolate using liquid chromatography-tandem mass spectrometry (LC-MS/MS)
    • DOI 10.1021/jf060714e
    • Shefcheck, K. J., J. H. Callahan, and S. M. Musser. 2006. Confirmation of peanut protein using peptide markers in dark chocolate using liquid chromatography-tandem mass spectrometry (LC-MS/MS). J. Agric. Food Chem. 54:7953-7959. (Pubitemid 44785369)
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.21 , pp. 7953-7959
    • Shefcheck, K.J.1    Callahan, J.H.2    Musser, S.M.3
  • 311
    • 2442583609 scopus 로고    scopus 로고
    • Confirmation of the allergenic peanut protein, Ara h 1, in a model food matrix using liquid chromatography/tandem mass spectrometry (LC/MS/MS)
    • Shefcheck, K. J., and S. M. Musser. 2004. Confirmation of the allergenic peanut protein, Ara h 1, in a model food matrix using liquid chromatography/tandem mass spectrometry (LC/MS/MS). J. Agric. Food Chem. 52:2785-2790.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 2785-2790
    • Shefcheck, K.J.1    Musser, S.M.2
  • 312
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., H. Tomas, J. Havlis, J. V. Olsen, and M. Mann. 2006. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1:2856-2860.
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 313
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 315
    • 5644226254 scopus 로고    scopus 로고
    • The role of liquid chromatography in proteomics
    • DOI 10.1016/j.chroma.2004.07.044, PII S002196730401204X
    • Shi, Y., R. Xiang, C. Horváth, and J. A. Wilkins. 2004. The role of liquid chromatography in proteomics. J. Chromatogr. A 1053:27-36. (Pubitemid 39369757)
    • (2004) Journal of Chromatography A , vol.1053 , Issue.1-2 SPEC. ISS. , pp. 27-36
    • Shi, Y.1    Xiang, R.2    Horvath, C.3    Wilkins, J.A.4
  • 316
    • 40549109531 scopus 로고    scopus 로고
    • Quantitative detection of allergenic protein Sin a 1 from yellow mustard (Sinapis alba l.) seeds using enzyme-linked immunosorbent assay
    • DOI 10.1021/jf072660u
    • Shim, Y. Y., and J. P. Wanasundara. 2008. Quantitative detection of allergenic protein Sin a 1 from yellow mustard (Sinapis alba L.) seeds using enzyme-linked immunosorbent assay. J. Agric. Food Chem. 56:1184-1192. (Pubitemid 351364046)
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.4 , pp. 1184-1192
    • Shim, Y.-Y.1    Wanasundara, J.P.D.2
  • 317
    • 72449198474 scopus 로고    scopus 로고
    • nsLTP and profilin are allergens in mustard seeds: Cloning, sequencing and recombinant production of Sin a 3 and Sin a 4
    • Sirvent, S., O. Palomares, A. Vereda, M. Villalba, J. Cuesta-Herranz, and R. Rodríguez. 2009. nsLTP and profilin are allergens in mustard seeds: cloning, sequencing and recombinant production of Sin a 3 and Sin a 4. Clin. Exp. Allergy 39:1929-1936.
    • (2009) Clin. Exp. Allergy , vol.39 , pp. 1929-1936
    • Sirvent, S.1    Palomares, O.2    Vereda, A.3    Villalba, M.4    Cuesta-Herranz, J.5    Rodríguez, R.6
  • 318
    • 0031937361 scopus 로고    scopus 로고
    • Isolation and functionality testing of low molecular weight glutenin subunits
    • Sissons, M. J., F. Bekes, and J. H. Skerritt. 1998. Isolation and functionality testing of low molecular weight glutenin subunits. Cereal Chem. 75:30-35.
    • (1998) Cereal Chem. , vol.75 , pp. 30-35
    • Sissons, M.J.1    Bekes, F.2    Skerritt, J.H.3
  • 319
    • 0026612067 scopus 로고
    • Purification and characterisation of antigenic gliadins in coeliac disease
    • Sjöström, H., S. U. Friis, O. Norén, and D. Anthonsen. 1992. Purification and characterisation of antigenic gliadins in coeliac disease. Clin. Chim. Acta 207:227-237.
    • (1992) Clin. Chim. Acta , vol.207 , pp. 227-237
    • Sjöström, H.1    Friis, S.U.2    Norén, O.3    Anthonsen, D.4
  • 320
    • 0033230075 scopus 로고    scopus 로고
    • Use of mass spectrometry to rapidly characterize the heterogeneity of bovine a-lactalbumin
    • Slangen, C. J., and S. Visser. 1999. Use of mass spectrometry to rapidly characterize the heterogeneity of bovine a-lactalbumin. J. Agric. Food Chem. 47:4549-4556.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4549-4556
    • Slangen, C.J.1    Visser, S.2
  • 321
    • 0036049889 scopus 로고    scopus 로고
    • Quantitative protein profiling using two-dimensional gel electrophoresis, isotope-coded affinity tag labeling, and mass spectrometry
    • Smolka, M., H. Zhou, and R. Aebersold. 2002. Quantitative protein profiling using two-dimensional gel electrophoresis, isotope-coded affinity tag labeling, and mass spectrometry. Mol. Cell. Proteomics 1:19-29.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 19-29
    • Smolka, M.1    Zhou, H.2    Aebersold, R.3
  • 322
    • 58149189256 scopus 로고    scopus 로고
    • Sequence analysis and expression of a cDNA clone encoding tropomysin in Sinonovacula constricta
    • Song, J., L. Li, Z. Liu, Q. Li, and P. Ran. 2009. Sequence analysis and expression of a cDNA clone encoding tropomysin in Sinonovacula constricta. Mol. Biol. Rep. 36:315-321.
    • (2009) Mol. Biol. Rep. , vol.36 , pp. 315-321
    • Song, J.1    Li, L.2    Liu, Z.3    Li, Q.4    Ran, P.5
  • 323
    • 67349232469 scopus 로고    scopus 로고
    • IgE-binding epitopic peptide mapping on a three-dimensional model built for the 13S globulin allergen of buckwheat (Fagopyrum esculentum)
    • Sordet, C., R. Culerrier, C. Granier, A. Didier, and R. Rougé. 2009. IgE-binding epitopic peptide mapping on a three-dimensional model built for the 13S globulin allergen of buckwheat (Fagopyrum esculentum). Peptides 30:1021-1027.
    • (2009) Peptides , vol.30 , pp. 1021-1027
    • Sordet, C.1    Culerrier, R.2    Granier, C.3    Didier, A.4    Rougé, R.5
  • 324
    • 0141631283 scopus 로고    scopus 로고
    • Variety identification of wheat using mass spectrometry with neural networks and the influence of mass spectra processing prior to neural network analysis
    • DOI 10.1002/rcm.709
    • Sørensen, H. A., M. M. Sperotto, M. Petersen, C. Kemir, L. Radzikowski, S. Jacobsen, and I. Søndergaard. 2002. Variety identification of wheat using mass spectrometry with neural networks and the influence of mass spectra processing prior to neural network analysis. Rapid Commun. Mass Spectrom. 16:1232-1237. (Pubitemid 34619586)
    • (2002) Rapid Communications in Mass Spectrometry , vol.16 , Issue.12 , pp. 1232-1237
    • Sorensen, H.A.1    Sperotto, M.M.2    Petersen, M.3    Kesmir, C.4    Radzikowski, L.5    Jacobsen, S.6    Sondergaard, I.7
  • 326
    • 63649131272 scopus 로고    scopus 로고
    • Validation of gel-free, label-free quantitative proteomics approaches: Applications for seed allergen profiling
    • Stevenson, S. E., Y. Chu, P. Ozias-Akins, and J. J. Thelen. 2009. Validation of gel-free, label-free quantitative proteomics approaches: applications for seed allergen profiling. J. Proteomics 72:555-566.
    • (2009) J. Proteomics , vol.72 , pp. 555-566
    • Stevenson, S.E.1    Chu, Y.2    Ozias-Akins, P.3    Thelen, J.J.4
  • 327
    • 0027066793 scopus 로고
    • Chromatographic and electrophoretic methods used for analysis of milk proteins
    • DOI 10.1016/0021-9673(92)85675-J
    • Strange, E. D., E. L. Malin, D. L. Van Hekken, and J. J. Basch. 1992. Chromatographic and electrophoretic methods used for analysis of milk proteins. J. Chromatogr. 624:81-102. (Pubitemid 23008606)
    • (1992) Journal of Chromatography , vol.624 , Issue.1-2 , pp. 81-102
    • Strange, E.D.1    Malin, E.L.2    Van Hekken, D.L.3    Basch, J.J.4
  • 330
    • 0036419889 scopus 로고    scopus 로고
    • Pepsin-resistant 16-kD buckwheat protein is associated with immediate hypersensitivity reaction in patients with buckwheat allergy
    • DOI 10.1159/000065173
    • Tanaka, K., K. Matsumoto, A. Akasawa, T. Nakajima, T. Nagasu, Y. Iikura, and H. Saito. 2002. Pepsin-resistant 16-kD buckwheat protein is associated with immediate hypersensitivity reaction in patients with buckwheat allergy. Int. Arch. Allergy Immunol. 129: 49-56. (Pubitemid 35316848)
    • (2002) International Archives of Allergy and Immunology , vol.129 , Issue.1 , pp. 49-56
    • Tanaka, K.1    Matsumoto, K.2    Akasawa, A.3    Nakajima, T.4    Nagasu, T.5    Iikura, Y.6    Saito, H.7
  • 331
    • 70349649363 scopus 로고    scopus 로고
    • Purification process for the preparation and characterizations of hen egg white ovalbumin, lysozyme, ovotransferrin, and ovomucoid
    • Tankrathok, A., S. Daduang, R. Patramanon, T. Araki, and S. Thammasirirak. 2009. Purification process for the preparation and characterizations of hen egg white ovalbumin, lysozyme, ovotransferrin, and ovomucoid. Prep. Biochem. Biotechnol. 39:380-399.
    • (2009) Prep. Biochem. Biotechnol. , vol.39 , pp. 380-399
    • Tankrathok, A.1    Daduang, S.2    Patramanon, R.3    Araki, T.4    Thammasirirak, S.5
  • 333
    • 0036310862 scopus 로고    scopus 로고
    • Harmonized guidelines for single-laboratory validation of methods of analysis
    • Thompson, M., S. L. R. Ellison, and R. Wood. 2002. Harmonized guidelines for single-laboratory validation of methods of analysis. IUPAC technical report. Pure Appl. Chem. 74:835-855.
    • (2002) IUPAC technical report. Pure Appl. Chem. , vol.74 , pp. 835-855
    • Thompson, M.1    Ellison, S.L.R.2    Wood, R.3
  • 334
    • 33644745259 scopus 로고    scopus 로고
    • Identification of proteins in Renaissance paintings by proteomics
    • DOI 10.1021/ac051181w
    • Tokarski, C., E. Martin, C. Rolando, and C. Cren-Olivé. 2006. Identification of proteins in Renaissance paintings by proteomics. Anal. Chem. 78:1494-1502. (Pubitemid 43346285)
    • (2006) Analytical Chemistry , vol.78 , Issue.5 , pp. 1494-1502
    • Tokarski, C.1    Martin, E.2    Rolando, C.3    Cren-Olive, C.4
  • 335
    • 33846191632 scopus 로고    scopus 로고
    • Requirements for prediction of peptide retention time in reversed-phase high-performance liquid chromatography: Hydrophilicity/hydrophobicity of side-chains at the N- and C-termini of peptides are dramatically affected by the end-groups and location
    • DOI 10.1016/j.chroma.2006.12.024, PII S0021967306023156
    • Tripet, B., D. Cepeniene, J. M. Kovacs, C. T. Mant, O. V. Krokhin, and R. S. Hodges. 2007. Requirements for prediction of peptide retention time in reversed-phase high-performance liquid chromatography: hydrophilicity/ hydrophobicity of side-chains at the N-and C-termini of peptides are dramatically affected by the end-groups and location. J. Chromatogr. A 1141:212-225. (Pubitemid 46096969)
    • (2007) Journal of Chromatography A , vol.1141 , Issue.2 , pp. 212-225
    • Tripet, B.1    Cepeniene, D.2    Kovacs, J.M.3    Mant, C.T.4    Krokhin, O.V.5    Hodges, R.S.6
  • 336
    • 0033629739 scopus 로고    scopus 로고
    • Analysis of major caprine milk proteins by reverse-phase high-performance liquid chromatography and electrospray ionization-mass spectrometry
    • Trujillo, A. J., I. Casals, and B. Guamis. 2000. Analysis of major caprine milk proteins by reverse-phase high-performance liquid chromatography and electrospray ionization-mass spectrometry. J. Dairy Sci. 83:11-19.
    • (2000) J. Dairy Sci. , vol.83 , pp. 11-19
    • Trujillo, A.J.1    Casals, I.2    Guamis, B.3
  • 337
    • 0033968011 scopus 로고    scopus 로고
    • Analysis of major ovine milk proteins by reversed-phase high-performance liquid chromatography and flow injection analysis with electrospray ionization mass spectrometry
    • DOI 10.1016/S0021-9673(99)01097-3, PII S0021967399010973
    • Trujillo, A. J., I. Casals, and B. Guamis. 2000. Analysis of major ovine milk proteins by reversed-phase high-performance liquid chromatography and flow injection analysis with electrospray ionization mass spectrometry. J. Chromatogr. A 870:371-380. (Pubitemid 30077439)
    • (2000) Journal of Chromatography A , vol.870 , Issue.1-2 , pp. 371-380
    • Trujillo, A.-J.1    Casals, I.2    Guamis, B.3
  • 338
    • 2942718871 scopus 로고    scopus 로고
    • New protease inhibitors from buckwheat seeds: Properties, partial amino acid sequences and possible biological role
    • DOI 10.1515/BC.2004.049
    • Tsybina, T., Y. Dunaevsky, A. Musolyamov, T. Egorov, N. Larionova, N. Popykina, and M. Belozersky. 2004. New protease inhibitors from buckwheat seeds: properties, partial amino acid sequences and possible biological role. Biol. Chem. 385:429-434. (Pubitemid 38787123)
    • (2004) Biological Chemistry , vol.385 , Issue.5 , pp. 429-434
    • Tsybina, T.1    Dunaevsky, Y.2    Musolyamov, A.3    Egorov, T.4    Larionova, N.5    Popykina, N.6    Belozersky, M.7
  • 341
    • 0028861499 scopus 로고
    • Isolation of hen egg white lysozyme, ovotransferrin and ovalbumin, using a quaternary ammonium bound to a highly crosslinked agarose matrix
    • Vachier, M. C., M. Piot, and A. C. Awadé. 1995. Isolation of hen egg white lysozyme, ovotransferrin and ovalbumin, using a quaternary ammonium bound to a highly crosslinked agarose matrix. J. Chromatogr. B 664:201-210.
    • (1995) J. Chromatogr. B , vol.664 , pp. 201-210
    • Vachier, M.C.1    Piot, M.2    Awadé, C.A.3
  • 342
    • 0035891934 scopus 로고    scopus 로고
    • Multidimensional separations of complex peptide mixtures: A combined high-performance liquid chromatography/ion mobility/time-of-flight mass spectrometry approach
    • Valentine, S. J., M. Kulchania, C. A. Srebalus Barnes, and D. E. Clemmer. 2001. Multidimensional separations of complex peptide mixtures: a combined high-performance liquid chromatography/ion mobility/time-of-flight mass spectrometry approach. Int. J. Mass Spectrom. 212:97-109.
    • (2001) Int. J. Mass Spectrom. , vol.212 , pp. 97-109
    • Valentine, S.J.1    Kulchania, M.2    Srebalus Barnes, C.A.3    Clemmer, E.D.4
  • 344
    • 0037162919 scopus 로고    scopus 로고
    • Separation and quantification of the major casein fractions by reverse-phase high-performance liquid chromatography and urea-polyacrylamide gel electrophoresis: Detection of milk adulterations
    • DOI 10.1016/S0021-9673(02)00787-2, PII S0021967302007872
    • Veloso, A. C., N. Teixeira, and I. M. Ferreira. 2002. Separation and quantification of the major casein fractions by reverse-phase highperformance liquid chromatography and urea-polyacrylamide gel electrophoresis. Detection of milk adulterations. J. Chromatogr. A 967:209-218. (Pubitemid 34808712)
    • (2002) Journal of Chromatography A , vol.967 , Issue.2 , pp. 209-218
    • Veloso, A.C.A.1    Teixeira, N.2    Ferreira, I.M.P.L.V.O.3
  • 345
    • 0038100072 scopus 로고    scopus 로고
    • Identification of wheat endosperm proteins by MALDI mass spectrometry and LC-MS/MS
    • Vensel, W., L. Harden, C. Tanaka, W. Hurkman, and W. Haddon. 2002. Identification of wheat endosperm proteins by MALDI mass spectrometry and LC-MS/MS. J. Biomol. Tech. 13:95-100.
    • (2002) J. Biomol. Tech. , vol.13 , pp. 95-100
    • Vensel, W.1    Harden, L.2    Tanaka, C.3    Hurkman, W.4    Haddon, W.5
  • 346
    • 17844403012 scopus 로고    scopus 로고
    • Developmental changes in the metabolic protein profiles of wheat endosperm
    • DOI 10.1002/pmic.200401034
    • Vensel, W. H., C. K. Tanaka, N. Cai, J. H. Wong, B. B. Buchanan, and W. J. Hurkman. 2005. Developmental changes in the metabolic protein profiles of wheat endosperm. Proteomics 5:1594-1611. (Pubitemid 40593267)
    • (2005) Proteomics , vol.5 , Issue.6 , pp. 1594-1611
    • Vensel, W.H.1    Janaka, C.K.2    Cai, N.3    Wong, J.H.4    Buchanan, B.B.5    Hurkman, W.J.6
  • 347
    • 0025775216 scopus 로고
    • Phenotyping of bovine milk proteins by reversed-phase high-performance liquid chromatography
    • Visser, S., C. J. Slangen, and H. S. Rollema. 1991. Phenotyping of bovine milk proteins by reversed-phase high-performance liquid chromatography. J. Chromatogr. 548:361-370.
    • (1991) J. Chromatogr. , vol.548 , pp. 361-370
    • Visser, S.1    Slangen, C.J.2    Rollema, S.H.3
  • 350
    • 68949145941 scopus 로고    scopus 로고
    • Emerging analytical methods to determine gluten markers in processed foods-method development in support of standard setting
    • Weber, D., C. Cléroux, and S. B. Godefroy. 2009. Emerging analytical methods to determine gluten markers in processed foods-method development in support of standard setting. Anal. Bioanal. Chem. 395:111-117.
    • (2009) Anal. Bioanal. Chem. , vol.395 , pp. 111-117
    • Weber, D.1    Cléroux, C.2    Godefroy, B.S.3
  • 351
    • 84858698710 scopus 로고    scopus 로고
    • Detection and confirmation of food allergen using mass spectrometric techniques: Characterization of allergens in hazelnut using esi and maldi mass spectrometry
    • F. A. Al-Taher, L. Jackson, and J. W. DeVries (ed.), ACS Publications, Washington, DC
    • Weber, D., G. Polenta, B. P.-Y. Lau, and S. B. Godefroy. 2009. Detection and confirmation of food allergen using mass spectrometric techniques: characterization of allergens in hazelnut using ESI and MALDI mass spectrometry, p. 153-182. In F. A. Al-Taher, L. Jackson, and J. W. DeVries (ed.), Intentional and unintentional contaminants in food and feed, vol. 1020. ACS Publications, Washington, DC.
    • (2009) Intentional and Unintentional Contaminants in Food and Feed , vol.1020 , pp. 153-182
    • Weber, D.1    Polenta, G.2    Lau, B.P.-Y.3    Godefroy, B.S.4
  • 352
    • 33645459558 scopus 로고    scopus 로고
    • Development of a liquid chromatography-tandem mass spectrometry method using capillary liquid chromatography and nanoelectrospray ionization-quadrupole time-of-flight hybrid mass spectrometer for the detection of milk allergens
    • Weber, D., P. Raymond, S. Ben-Rejeb, and B. Lau. 2006. Development of a liquid chromatography-tandem mass spectrometry method using capillary liquid chromatography and nanoelectrospray ionization-quadrupole time-of-flight hybrid mass spectrometer for the detection of milk allergens. J. Agric. Food Chem. 54:1604-1610.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 1604-1610
    • Weber, D.1    Raymond, P.2    Ben-Rejeb, S.3    Lau, B.4
  • 353
    • 6044226889 scopus 로고    scopus 로고
    • Differential mass spectrometry: A label-free LC-MS method for finding significant differences in complex peptide and protein mixtures
    • DOI 10.1021/ac0493875
    • Wiener, M. C., J. R. Sachs, E. G. Deyanova, and N. A. Yates. 2004. Differential mass spectrometry: a label-free LC-MS method for finding significant differences in complex peptide and protein mixtures. Anal. Chem. 76:6085-6096. (Pubitemid 39382956)
    • (2004) Analytical Chemistry , vol.76 , Issue.20 , pp. 6085-6096
    • Wiener, M.C.1    Sachs, J.R.2    Deyanova, E.G.3    Yates, N.A.4
  • 354
    • 0031696005 scopus 로고    scopus 로고
    • Quantitative determination of gluten protein types in wheat flour by reversed-phase high-performance liquid chromatography
    • Wieser, H., S. Antes, and W. Seilmeier. 1998. Quantitative determination of gluten protein types in wheat flour by reversedphase high-performance liquid chromatography. Cereal Chem. 75: 644-650. (Pubitemid 28456336)
    • (1998) Cereal Chemistry , vol.75 , Issue.5 , pp. 644-650
    • Wieser, H.1    Antes, S.2    Seilmeier, W.3
  • 355
    • 0003041253 scopus 로고
    • Quantitative determination of gliadin subgroups from different wheat cultivars
    • Wieser, H., W. Seilmeier, and H.-D. Belitz. 1994. Quantitative determination of gliadin subgroups from different wheat cultivars. J. Cereal Sci. 19:149-155.
    • (1994) J. Cereal Sci. , vol.19 , pp. 149-155
    • Wieser, H.1    Seilmeier, W.2    Belitz, H.-D.3
  • 356
    • 0342990269 scopus 로고
    • Preparative reversed-phase high-performance liquid chromatography of soybean proteins and characterization of fractions by gel electrophoresis
    • Wolf, W. J., R. E. Peterson, and M. L. Schaer. 1992. Preparative reversed-phase high-performance liquid chromatography of soybean proteins and characterization of fractions by gel electrophoresis. J. Agric. Food Chem. 40:1809-1816.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 1809-1816
    • Wolf, W.J.1    Peterson, R.E.2    Schaer, L.M.3
  • 358
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF
    • DOI 10.1021/pr050405o
    • Wu, W. W., G. Wang, S. J. Baek, and R. F. Shen. 2006. Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel-or LC-MALDI TOF/TOF. J. Proteome Res. 5:651-658. (Pubitemid 43364106)
    • (2006) Journal of Proteome Research , vol.5 , Issue.3 , pp. 651-658
    • Wu, W.W.1    Wang, G.2    Baek, S.J.3    Shen, R.-F.4
  • 359
    • 0035131818 scopus 로고    scopus 로고
    • Antifreeze glycoproteins: Relationship between molecular weight, thermal hysteresis and the inhibition of leakage from liposomes during thermotropic phase transition
    • DOI 10.1016/S1096-4959(00)00323-7, PII S1096495900003237
    • Wu, Y., J. Banoubb, S. V. Goddard, M. H. Kao, and G. L. Fletcher. 2001. Antifreeze glycoproteins: relationship between molecular weight, thermal hysteresis and the inhibition of leakage from liposomes during thermotropic phase transition. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 128:265-273. (Pubitemid 32157516)
    • (2001) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology , vol.128 , Issue.2 , pp. 265-273
    • Wu, Y.1    Banoub, J.2    Goddard, S.V.3    Kao, M.H.4    Fletcher, G.L.5
  • 360
    • 13844275962 scopus 로고    scopus 로고
    • Mass spectrometry of peptides and proteins
    • DOI 10.1016/j.ymeth.2004.08.013
    • Wysocki, V. H., K. A. Resing, Q. Zhang, and G. Cheng. 2005. Mass spectrometry of peptides and proteins. Methods 35:211-222. (Pubitemid 40255587)
    • (2005) Methods , vol.35 , Issue.3 SPEC.ISS. , pp. 211-222
    • Wysocki, V.H.1    Resing, K.A.2    Zhang, Q.3    Cheng, G.4
  • 361
    • 0000668858 scopus 로고
    • Isolation and partial characterization of a salt-extractable globulin from soybean seeds
    • Yamauchi, F., K. Sato, and T. Yamagishi. 1994. Isolation and partial characterization of a salt-extractable globulin from soybean seeds. Agric. Biol. Chem. 48:645-650.
    • (1994) Agric. Biol. Chem. , vol.48 , pp. 645-650
    • Yamauchi, F.1    Sato, K.2    Yamagishi, T.3
  • 362
    • 0001603894 scopus 로고
    • Purification and properties of allergenic proteins in buckwheat seeds
    • Yano, M., R. Nakamura, S. Hayakawara, and S. Torii. 1989. Purification and properties of allergenic proteins in buckwheat seeds. Agric. Biol. Chem. 53:2387-2392.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2387-2392
    • Yano, M.1    Nakamura, R.2    Hayakawara, S.3    Torii, S.4
  • 363
    • 0033764222 scopus 로고    scopus 로고
    • Electrophoretic and immunochemical characterization of allergenic proteins in buckwheat
    • Yoshimasu, M. A., J. W. Zhang, S. Hayakawa, and Y. Mine. 2000. Electrophoretic and immunochemical characterization of allergenic proteins in buckwheat. Int. Arch. Allergy Immunol. 123:130-136.
    • (2000) Int. Arch. Allergy Immunol. , vol.123 , pp. 130-136
    • Yoshimasu, M.A.1    Zhang, J.W.2    Hayakawa, S.3    Mine, Y.4
  • 364
    • 0037223013 scopus 로고    scopus 로고
    • Proteomics and immunological analysis of a novel shrimp allergen
    • Yu, C. J., Y. F. Lin, B. L. Chiang, and L. P. Chow. 2003. Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. J. Immunol. 170:445-453.
    • (2003) Pen m 2. J. Immunol. , vol.170 , pp. 445-453
    • Yu, C.J.1    Lin, Y.F.2    Chiang, B.L.3    Chow, L.P.4
  • 365
    • 0034512031 scopus 로고    scopus 로고
    • Haemoglobin sturucture and biochemical characteristic of the sulphide-binding component from the deep-sea clam Calyyptogena magnifica
    • Zal, F., E. Leize, D. R. Oros, S. Hourdez, A. Van Dorsselaer, and J. J. Childress. 2000. Haemoglobin structure and biochemical characteristics of the sulphide-binding component from the deepsea clam Calyptogena magnifica. Cah. Biol. Mar. 41:413-423. (Pubitemid 32113924)
    • (2000) Cahiers de Biologie Marine , vol.41 , Issue.4 , pp. 413-423
    • Zal, F.1    Leize, E.2    Oros, D.R.3    Hourdez, S.4    Dorsselaers, A.V.5    Childless, J.J.6
  • 366
    • 0032078077 scopus 로고    scopus 로고
    • Identification of C-terminally truncated forms of β-lactoglobulin in whey from Romagnola cows' milk by two dimensional electrophoresis coupled to mass spectrometry
    • DOI 10.1017/S0022029997002859
    • Zappacosta, F., A. Di Luccia, L. Ledda, and F. Addeo. 1998. Identification of C-terminally truncated forms of β-lactoglobulin in whey from Romagnola cows' milk by two dimensional electrophoresis coupled to mass spectrometry. J. Dairy Res. 65:243-252. (Pubitemid 28235899)
    • (1998) Journal of Dairy Research , vol.65 , Issue.2 , pp. 243-252
    • Zappacosta, F.1    Di Luccia, A.2    Ledda, L.3    Addeo, F.4
  • 367
    • 39649084426 scopus 로고    scopus 로고
    • Characterization of HMW glutenin subunits in common wheat and related species by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS)
    • DOI 10.1016/j.jcs.2007.04.013, PII S0733521007000707
    • Zhang, Q., Y. Dong, X. An, A. Wang, Y. Zhang, X. Li, L. Gao, X. Xia, Z. He, and Y. Yan. 2008. Characterization of HMW glutenin subunits in common wheat and related species by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). J. Cereal Sci. 47:252-261. (Pubitemid 351288995)
    • (2008) Journal of Cereal Science , vol.47 , Issue.2 , pp. 252-261
    • Zhang, Q.1    Dong, Y.2    An, X.3    Wang, A.4    Zhang, Y.5    Li, X.6    Gao, L.7    Xia, X.8    He, Z.9    Yan, Y.10
  • 368
    • 1842816565 scopus 로고    scopus 로고
    • Identification of a type of human IgG-like protein in shrimp Penaeus vannamei by mass spectrometry
    • DOI 10.1016/j.jembe.2003.09.011, PII S0022098103004684
    • Zhang, Y., S. Wang, and X. Peng. 2004. Identification of a type of human IgG-like protein in shrimp Penaeus vannamei by mass spectrometry. J. Exp. Mar. Biol. Ecol. 301:39-54. (Pubitemid 38473540)
    • (2004) Journal of Experimental Marine Biology and Ecology , vol.301 , Issue.1 , pp. 39-54
    • Zhang, Y.1    Wang, S.2    Peng, X.3


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