메뉴 건너뛰기




Volumn 9, Issue 2, 2009, Pages 272-286

A label-free internal standard method for the differential analysis of bioactive lupin proteins using nano HPLC-Chip coupled with Ion Trap mass spectrometry

Author keywords

Differential analysis; HPLC Chip; Label free; Lupin protein; MS

Indexed keywords

AMINO ACID; ION; LUPIN PROTEIN; PEPTIDE; PROTEOME; STABLE ISOTOPE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; VICILIN;

EID: 60349105480     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800317     Document Type: Article
Times cited : (51)

References (36)
  • 1
    • 1542380561 scopus 로고    scopus 로고
    • Proteomics: Present and future in food quality evaluation
    • Carbonaro, M., Proteomics: Present and future in food quality evaluation. Trends Food Technol. 2004, 15, 209-216.
    • (2004) Trends Food Technol , vol.15 , pp. 209-216
    • Carbonaro, M.1
  • 2
    • 33646473345 scopus 로고    scopus 로고
    • Mammalian organelle map by protein correlation profiling
    • Foster, L., de Hoog, C. L., Zhang, Y., Xie, X. et al., Mammalian organelle map by protein correlation profiling. Cell 2006, 125, 187-199.
    • (2006) Cell , vol.125 , pp. 187-199
    • Foster, L.1    de Hoog, C.L.2    Zhang, Y.3    Xie, X.4
  • 3
    • 33846133955 scopus 로고    scopus 로고
    • Computational prediction of proteotypic peptides for quantitative proteomics
    • Mallick, P., Schirle, M., Chen, S. S., Flory, M. R. et al., Computational prediction of proteotypic peptides for quantitative proteomics. Nat. Biotechnol. 2007, 25, 125-131.
    • (2007) Nat. Biotechnol , vol.25 , pp. 125-131
    • Mallick, P.1    Schirle, M.2    Chen, S.S.3    Flory, M.R.4
  • 4
    • 27644543078 scopus 로고    scopus 로고
    • Comparison of label-free methods for quantifying human proteins by shotgun proteomics
    • Old, W. M., Meyer-Arendt, K., Aveline-Wolf, L., Pierce, K. G. et al., Comparison of label-free methods for quantifying human proteins by shotgun proteomics. Mol. Cell Proteomics 2005, 4, 1487-1502.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1487-1502
    • Old, W.M.1    Meyer-Arendt, K.2    Aveline-Wolf, L.3    Pierce, K.G.4
  • 5
    • 24044467381 scopus 로고    scopus 로고
    • Analysis of phospho-protein dynamics in a B cell lymphoma cell line
    • Quantification of gel-separated proteins and their phophorylation sites by LC-MS using unlabeled internal standards
    • Cutillas, P. R., Geering, B., Waterfield, M. D., Vanhaesebroeck, B., Quantification of gel-separated proteins and their phophorylation sites by LC-MS using unlabeled internal standards: Analysis of phospho-protein dynamics in a B cell lymphoma cell line. Mol. Cell Proteomics 2005, 4, 1038-1051.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1038-1051
    • Cutillas, P.R.1    Geering, B.2    Waterfield, M.D.3    Vanhaesebroeck, B.4
  • 6
    • 31044434492 scopus 로고    scopus 로고
    • Optimization of a pilot scale process for producing lupin protein isolates with valuable technological properties and minimum thermal damage
    • D'Agostina, A., Antonioni, C., Resta, D., Arnoldi, A. et al., Optimization of a pilot scale process for producing lupin protein isolates with valuable technological properties and minimum thermal damage. J. Agric. Food Chem. 2006, 54, 92-98.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 92-98
    • D'Agostina, A.1    Antonioni, C.2    Resta, D.3    Arnoldi, A.4
  • 7
    • 34447536821 scopus 로고    scopus 로고
    • Thermal damage and availability of potentially hypocolesterolemic peptides in lupin-based ingredients and food products
    • Arnoldi, A., Resta, D., Brambilla, F., Boschin, G. et al., Thermal damage and availability of potentially hypocolesterolemic peptides in lupin-based ingredients and food products. Mol. Nutr. Food Res. 2007, 51, 431-436.
    • (2007) Mol. Nutr. Food Res , vol.51 , pp. 431-436
    • Arnoldi, A.1    Resta, D.2    Brambilla, F.3    Boschin, G.4
  • 8
    • 0346726203 scopus 로고    scopus 로고
    • Proteins of white lupin seed-a natural isoflavone poor legume-reduce LDL in rats and increase LDL receptor activity
    • Sirtori, C. R., Lovati, M. R., Manzoni, C., Castiglioni, S. et al., Proteins of white lupin seed-a natural isoflavone poor legume-reduce LDL in rats and increase LDL receptor activity. J. Nutr. 2004, 134, 18-23.
    • (2004) J. Nutr , vol.134 , pp. 18-23
    • Sirtori, C.R.1    Lovati, M.R.2    Manzoni, C.3    Castiglioni, S.4
  • 9
    • 24744447822 scopus 로고    scopus 로고
    • Cholesterol-lowering effects of dietary blue lupin (Lupinus angustifolius L.) in intact and ileorectal anastomosed pigs
    • Martins, J. M., Riottot, M., De Abreu, M. C., Viegas-Crespo, A. M. et al., Cholesterol-lowering effects of dietary blue lupin (Lupinus angustifolius L.) in intact and ileorectal anastomosed pigs. J. Lipid Res. 2005, 46, 1539-1547.
    • (2005) J. Lipid Res , vol.46 , pp. 1539-1547
    • Martins, J.M.1    Riottot, M.2    De Abreu, M.C.3    Viegas-Crespo, A.M.4
  • 10
    • 51749085387 scopus 로고    scopus 로고
    • Hypolipidaemic and anti-atherosclerotic effects of lupin proteins in rabbit model
    • Marchesi, M., Parolini, C., Diani, E., Rigamonti, E. et al., Hypolipidaemic and anti-atherosclerotic effects of lupin proteins in rabbit model. Brit. J. Nutr., 2008, 100, 707-710.
    • (2008) Brit. J. Nutr , vol.100 , pp. 707-710
    • Marchesi, M.1    Parolini, C.2    Diani, E.3    Rigamonti, E.4
  • 11
    • 10044254444 scopus 로고    scopus 로고
    • Conglutin gamma, a lupin seed protein, binds insulin in vitro and reduces plasma glucose levels of hyperglycemic rats
    • Magni, C., Sessa, F., Accardo, E., Vanoni, M. et al., Conglutin gamma, a lupin seed protein, binds insulin in vitro and reduces plasma glucose levels of hyperglycemic rats. J. Nutr. Biochem. 2004, 15, 646-650.
    • (2004) J. Nutr. Biochem , vol.15 , pp. 646-650
    • Magni, C.1    Sessa, F.2    Accardo, E.3    Vanoni, M.4
  • 12
    • 33746101496 scopus 로고    scopus 로고
    • Lupin protein attenuates the development of hypertension and normalises the vascular function of NaCl-loaded Goto-Kakizaki rats
    • Pilvi, T. K., Jauhiainen, T., Cheng, Z. J., Mervaala, E. M. et al., Lupin protein attenuates the development of hypertension and normalises the vascular function of NaCl-loaded Goto-Kakizaki rats. J. Physiol. Pharmacol. 2006, 57, 167-176.
    • (2006) J. Physiol. Pharmacol , vol.57 , pp. 167-176
    • Pilvi, T.K.1    Jauhiainen, T.2    Cheng, Z.J.3    Mervaala, E.M.4
  • 13
    • 0037326618 scopus 로고    scopus 로고
    • Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1)
    • Wensing, M., Knulst, A., Piersma, S., O'Kane, F. et al., Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1). J. Allergy Clin. Immunol. 2003, 111, 420-424.
    • (2003) J. Allergy Clin. Immunol , vol.111 , pp. 420-424
    • Wensing, M.1    Knulst, A.2    Piersma, S.3    O'Kane, F.4
  • 14
    • 20844438556 scopus 로고    scopus 로고
    • Analysis of Lupinus albus storage proteins by two-dimensional electrophoresis and mass spectrometry
    • Wait, R., Gianazza, R., Brambilla, D., Eberini, I. et al., Analysis of Lupinus albus storage proteins by two-dimensional electrophoresis and mass spectrometry. J. Agric. Food Chem. 2005, 53, 4599-4606.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 4599-4606
    • Wait, R.1    Gianazza, R.2    Brambilla, D.3    Eberini, I.4
  • 15
    • 2642556417 scopus 로고    scopus 로고
    • The α' subunit from soybean 7S globulin lowers plasma lipids and upregulates liver β-VLDL receptors in rats fed a hypercholesterolemic diet
    • Duranti, M., Lovati, M. R., Dani, V., Barbiroli, A. et al., The α' subunit from soybean 7S globulin lowers plasma lipids and upregulates liver β-VLDL receptors in rats fed a hypercholesterolemic diet. J. Nutr. 2004, 134, 1334-1339.
    • (2004) J. Nutr , vol.134 , pp. 1334-1339
    • Duranti, M.1    Lovati, M.R.2    Dani, V.3    Barbiroli, A.4
  • 16
    • 15444378641 scopus 로고    scopus 로고
    • Twodimensional electrophoresis and western blotting analyses with anti Ara h 3 basic subunit IgG evidence the crossreacting polypeptides of Arachis hypogaea, Glycine max and Lupinus albus seed proteomes
    • Magni, C., Ballabio, C., Restani, P., Sironi, E. et al., Twodimensional electrophoresis and western blotting analyses with anti Ara h 3 basic subunit IgG evidence the crossreacting polypeptides of Arachis hypogaea, Glycine max and Lupinus albus seed proteomes. J. Agric. Food Chem. 2005, 53, 2275-2281.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 2275-2281
    • Magni, C.1    Ballabio, C.2    Restani, P.3    Sironi, E.4
  • 18
    • 60349126130 scopus 로고    scopus 로고
    • High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics
    • Shen, Y., Zhao, R., Berger, S. J., Anderson, G. A. et al., High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics. Anal. Chem. 2002, 62, 882-899.
    • (2002) Anal. Chem , vol.62 , pp. 882-899
    • Shen, Y.1    Zhao, R.2    Berger, S.J.3    Anderson, G.A.4
  • 19
    • 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 semiquantitation of the main storage proteins of Lupinus albus in foods
    • Locati, D., Morandi, S., Zanotti, M., Arnoldi, A., Preliminary approaches for the development of a high performance liquid chromatography/electrospray ionization tandem mass spectrometry method for the detection and label/free semiquantitation of the main storage proteins of Lupinus albus in foods. Rapid Commun. Mass Spectrom. 2006, 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
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248.
    • (1976) Anal. Biochem , vol.72 , pp. 248
    • Bradford, M.1
  • 21
    • 33947190376 scopus 로고    scopus 로고
    • Combined 2-D electrophoretic approaches for the study of white lupin mature seed storage proteome
    • Magni, C., Scarafoni, A., Hernldl, A., Sessa, F. et al., Combined 2-D electrophoretic approaches for the study of white lupin mature seed storage proteome. Phytochemistry 2007, 68, 997-1007.
    • (2007) Phytochemistry , vol.68 , pp. 997-1007
    • Magni, C.1    Scarafoni, A.2    Hernldl, A.3    Sessa, F.4
  • 22
    • 33751517737 scopus 로고    scopus 로고
    • Vicilin-type globulins follow distinct patterns of degradation in different species of germinating legume seeds
    • Freitas, L. R., Teixeira, A. R., Ferreira, R. B., Vicilin-type globulins follow distinct patterns of degradation in different species of germinating legume seeds. Food Chem. 2007, 102, 323-329.
    • (2007) Food Chem , vol.102 , pp. 323-329
    • Freitas, L.R.1    Teixeira, A.R.2    Ferreira, R.B.3
  • 23
  • 24
    • 0142214654 scopus 로고    scopus 로고
    • Proteomics of Medicago truncatula seed development establishes the time frame of diverse metabolic processes related to reserve accumulation
    • Gallardo, K., Le Signor, C., Vandekerckhove, J.,Thomson, R. D., Burstin, J., Proteomics of Medicago truncatula seed development establishes the time frame of diverse metabolic processes related to reserve accumulation. Plant Physiol. 2003, 133, 664-682.
    • (2003) Plant Physiol , vol.133 , pp. 664-682
    • Gallardo, K.1    Le Signor, C.2    Vandekerckhove, J.3    Thomson, R.D.4    Burstin, J.5
  • 25
    • 0034979861 scopus 로고    scopus 로고
    • Proteomic analysis of Arabidopsis seed germination and priming
    • Gallardo, K., Job, C., Groot, S. P. C., Puype, M. et al., Proteomic analysis of Arabidopsis seed germination and priming. Plant Physiol. 2001, 126, 835-848.
    • (2001) Plant Physiol , vol.126 , pp. 835-848
    • Gallardo, K.1    Job, C.2    Groot, S.P.C.3    Puype, M.4
  • 26
    • 0035983666 scopus 로고    scopus 로고
    • Proteomics of Arabidopsis seed germination. A comparative study of wild-type and gibberellin-deficient seeds
    • Gallardo, K., Job, C., Groot, S. P. C., Puype, M. et al., Proteomics of Arabidopsis seed germination. A comparative study of wild-type and gibberellin-deficient seeds. Plant Physiol. 2002, 129, 823-837.
    • (2002) Plant Physiol , vol.129 , pp. 823-837
    • Gallardo, K.1    Job, C.2    Groot, S.P.C.3    Puype, M.4
  • 27
    • 20444449370 scopus 로고    scopus 로고
    • A systematic proteomic study of seed filling in soybean. Establishment of high-resolution two-dimentional reference maps, expression profiles, and interactive proteome database
    • Hajduch, M., Ganapathy, A., Stein, J. W., Thelen, J. J., A systematic proteomic study of seed filling in soybean. Establishment of high-resolution two-dimentional reference maps, expression profiles, and interactive proteome database. Plant Physiol. 2005, 137, 1397-1419.
    • (2005) Plant Physiol , vol.137 , pp. 1397-1419
    • Hajduch, M.1    Ganapathy, A.2    Stein, J.W.3    Thelen, J.J.4
  • 28
    • 0037330377 scopus 로고    scopus 로고
    • Proteomic analysis of the effect of heat stress on hexaploid wheat grain: Characterization of heat-responsive proteins from nonprolamins fraction
    • Majoul, T., Bacel, E., Ben Hamida, J., Branlard, G., Proteomic analysis of the effect of heat stress on hexaploid wheat grain: Characterization of heat-responsive proteins from nonprolamins fraction. Proteomics 2003, 3, 175-183.
    • (2003) Proteomics , vol.3 , pp. 175-183
    • Majoul, T.1    Bacel, E.2    Ben Hamida, J.3    Branlard, G.4
  • 29
    • 36448956829 scopus 로고    scopus 로고
    • Pseudo internal standard approach for label-free quantitative proteomics
    • Tabata, T., Sato, T., Kuromitsu, J., Oda, Y., Pseudo internal standard approach for label-free quantitative proteomics. Anal. Chem. 2007, 79, 8440-8445.
    • (2007) Anal. Chem , vol.79 , pp. 8440-8445
    • Tabata, T.1    Sato, T.2    Kuromitsu, J.3    Oda, Y.4
  • 30
    • 23944472666 scopus 로고    scopus 로고
    • Comprehensive label-free method for the relative quantification of proteins from biological samples
    • Higgs, R. E., Knierman, M. D., Gelfanova, V., Butler, J. P., Hale, J. E., Comprehensive label-free method for the relative quantification of proteins from biological samples. J. Proteome Res. 2005, 4, 1442-1450.
    • (2005) J. Proteome Res , vol.4 , pp. 1442-1450
    • Higgs, R.E.1    Knierman, M.D.2    Gelfanova, V.3    Butler, J.P.4    Hale, J.E.5
  • 31
    • 10744233766 scopus 로고    scopus 로고
    • Wang, W., Zhou, H., Lin, H., Roy, S. Quantification of proteins and metabolites by mass spectrometry without iso-topic labelling or spiked standards. Anal. Chem. 2003, 48184826.
    • Wang, W., Zhou, H., Lin, H., Roy, S. Quantification of proteins and metabolites by mass spectrometry without iso-topic labelling or spiked standards. Anal. Chem. 2003, 48184826.
  • 32
    • 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., Chelsius, D., Shaler, T. A., Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry. Anal. Chem. 2002, 74, 4741-4749.
    • (2002) Anal. Chem , vol.74 , pp. 4741-4749
    • Bondarenko, P.V.1    Chelsius, D.2    Shaler, T.A.3
  • 33
    • 4143107797 scopus 로고    scopus 로고
    • The urinary proteome in Fanconi syndrome implies specificity in the reabsorption of proteins by renal proximal tubule cells
    • Cutillas, P. R., Chalkley, R. J., Hansen, K., Cramer, R. et al., The urinary proteome in Fanconi syndrome implies specificity in the reabsorption of proteins by renal proximal tubule cells. Am. J. Physiol. 2004, 287, F353-F364.
    • (2004) Am. J. Physiol , vol.287
    • Cutillas, P.R.1    Chalkley, R.J.2    Hansen, K.3    Cramer, R.4
  • 34
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B. et al., Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127, 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4
  • 35
    • 34848822499 scopus 로고    scopus 로고
    • Quantitative profile of five murine core proteomes using label-free functional proteomics
    • Cutillas, P., Vanhaesebroeck, B., Quantitative profile of five murine core proteomes using label-free functional proteomics. Mol. Cell. Proteomics 2007, 1560-1573.
    • (2007) Mol. Cell. Proteomics , pp. 1560-1573
    • Cutillas, P.1    Vanhaesebroeck, B.2
  • 36
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assay for major plasma proteins
    • Anderson, L., Hunter, C. L., Quantitative mass spectrometric multiple reaction monitoring assay for major plasma proteins. Mol. Cell. Proteomics 2006, 5, 573-588.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.