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Volumn 1428, Issue , 2016, Pages 193-201

Labeling and label free shotgun proteomics approaches to characterize muscle tissue from farmed and wild gilthead sea bream (Sparus aurata)

Author keywords

Dimethyl labeling; Food fish proteome; Label free proteomics; Mass spectrometry; Quantification; Shotgun proteomics

Indexed keywords

FISH; MASS SPECTROMETRY; MUSCLE; PROTEINS;

EID: 84966495637     PISSN: 00219673     EISSN: 18733778     Source Type: Journal    
DOI: 10.1016/j.chroma.2015.07.049     Document Type: Article
Times cited : (55)

References (39)
  • 1
    • 84876678505 scopus 로고    scopus 로고
    • Health benefits of seafood; is it just the fatty acids?
    • Lund E.K. Health benefits of seafood; is it just the fatty acids?. Food Chem. 2013, 140:413-420.
    • (2013) Food Chem. , vol.140 , pp. 413-420
    • Lund, E.K.1
  • 3
    • 33746571529 scopus 로고    scopus 로고
    • Fatty acids in muscles and liver of Tunisian wild and farmed gilthead sea bream, Sparus aurata
    • Mnari A., Bouhlel I., Chraief I., Hammami M., Romdhane M.S., El Cafsi M., Chaouch A. Fatty acids in muscles and liver of Tunisian wild and farmed gilthead sea bream, Sparus aurata. Food Chem. 2007, 100:1393-1397.
    • (2007) Food Chem. , vol.100 , pp. 1393-1397
    • Mnari, A.1    Bouhlel, I.2    Chraief, I.3    Hammami, M.4    Romdhane, M.S.5    El Cafsi, M.6    Chaouch, A.7
  • 4
    • 84893153890 scopus 로고    scopus 로고
    • Proteomic profiling of sea bass muscle by two-dimensional gel electrophoresis and tandem mass spectrometry
    • Terova G., Pisanu S., Roggio T., Preziosa E., Saroglia M., Addis M.F. Proteomic profiling of sea bass muscle by two-dimensional gel electrophoresis and tandem mass spectrometry. Fish Physiol. Biochem. 2014, 30:311-322.
    • (2014) Fish Physiol. Biochem. , vol.30 , pp. 311-322
    • Terova, G.1    Pisanu, S.2    Roggio, T.3    Preziosa, E.4    Saroglia, M.5    Addis, M.F.6
  • 5
    • 84966675679 scopus 로고    scopus 로고
    • Seasonal variation of the chemical composition, fatty acid profiles and mineral elements of Diplodus annularis (Linnaeus 1758) caught in the Tunisian coastal water
    • Khitouni I.K., Mihoubi N.B., Bouain A., Rebah F.B. Seasonal variation of the chemical composition, fatty acid profiles and mineral elements of Diplodus annularis (Linnaeus 1758) caught in the Tunisian coastal water. J. Food Nutr. Res. 2014, 2:306-311.
    • (2014) J. Food Nutr. Res. , vol.2 , pp. 306-311
    • Khitouni, I.K.1    Mihoubi, N.B.2    Bouain, A.3    Rebah, F.B.4
  • 6
    • 0030858913 scopus 로고    scopus 로고
    • Influence of fish meal quality and feed pellet on growth, feed efficiency and muscle composition in gilthead seabream (Sparus aurata)
    • Aksnesa A., Izquierdo M.S., Robaina L., Vergara J.M., Montero D. Influence of fish meal quality and feed pellet on growth, feed efficiency and muscle composition in gilthead seabream (Sparus aurata). Aquaculture 1997, 153:251-261.
    • (1997) Aquaculture , vol.153 , pp. 251-261
    • Aksnesa, A.1    Izquierdo, M.S.2    Robaina, L.3    Vergara, J.M.4    Montero, D.5
  • 7
    • 33947301122 scopus 로고    scopus 로고
    • High resolution two-dimensional electrophoresis as a tool to differentiate wild from farmed cod (Gadus morhua) and to assess the protein composition of klipfish
    • Martinez I., Šliyte R., Daukŝas E. High resolution two-dimensional electrophoresis as a tool to differentiate wild from farmed cod (Gadus morhua) and to assess the protein composition of klipfish. Food Chem. 2007, 102:504-510.
    • (2007) Food Chem. , vol.102 , pp. 504-510
    • Martinez, I.1    Šlifyte, R.2    Daukŝas, E.3
  • 9
    • 84924692739 scopus 로고    scopus 로고
    • Nutriproteomics: facts, concepts, and perspectives
    • Sauer S., Luge T. Nutriproteomics: facts, concepts, and perspectives. Proteomics 2015, 15:997-1013.
    • (2015) Proteomics , vol.15 , pp. 997-1013
    • Sauer, S.1    Luge, T.2
  • 11
    • 84897378461 scopus 로고    scopus 로고
    • High-throughput proteomics: a new tool for quality and safety in fishery products
    • Tedesco S., Mullen W., Cristobal S. High-throughput proteomics: a new tool for quality and safety in fishery products. Curr. Protein Pept. Sci. 2014, 15:118-133.
    • (2014) Curr. Protein Pept. Sci. , vol.15 , pp. 118-133
    • Tedesco, S.1    Mullen, W.2    Cristobal, S.3
  • 14
    • 0038033771 scopus 로고    scopus 로고
    • Uncertainties and values in European aquaculture: communication, management and policy issues in times of "changing public perceptions"
    • Kaiser M., Stead S.M. Uncertainties and values in European aquaculture: communication, management and policy issues in times of "changing public perceptions". Aquacult Int. 2002, 10:469-490.
    • (2002) Aquacult Int. , vol.10 , pp. 469-490
    • Kaiser, M.1    Stead, S.M.2
  • 15
    • 84876076169 scopus 로고    scopus 로고
    • Comparative morphology of wild, farmed and hatchery released gilthead sea bream (Sparus aurata) in western Greece
    • Rogdakis Y.G., Koukou1 K.K., Ramfos A., Dimitriou E., Katselis G.N. Comparative morphology of wild, farmed and hatchery released gilthead sea bream (Sparus aurata) in western Greece. Int. J. Fish Aquac. 2011, 3:1-9.
    • (2011) Int. J. Fish Aquac. , vol.3 , pp. 1-9
    • Rogdakis, Y.G.1    Koukou1, K.K.2    Ramfos, A.3    Dimitriou, E.4    Katselis, G.N.5
  • 16
    • 84856394763 scopus 로고    scopus 로고
    • Comparison among different gilthead sea bream (Sparus aurata) farming systems: activity of intestinal and hepatic enzymes and 13C-NMR analysis of lipids
    • Del Coco L., Papadia P., De Pascali S.A., Bressani G., Storelli C., Zonno V., Fanizzi F.P. Comparison among different gilthead sea bream (Sparus aurata) farming systems: activity of intestinal and hepatic enzymes and 13C-NMR analysis of lipids. Nutrients 2009, 1:291-301.
    • (2009) Nutrients , vol.1 , pp. 291-301
    • Del Coco, L.1    Papadia, P.2    De Pascali, S.A.3    Bressani, G.4    Storelli, C.5    Zonno, V.6    Fanizzi, F.P.7
  • 17
    • 17644385255 scopus 로고    scopus 로고
    • Monitoring food quality by microfluidic electrophoresis, gas chromatography, and mass spectrometry techniques: effects of aquaculture on the sea bass (Dicentrarchus labrax)
    • Monti G., De Napoli L., Mainolfi P., Barone R., Guida M., Marino G., Amoresano A. Monitoring food quality by microfluidic electrophoresis, gas chromatography, and mass spectrometry techniques: effects of aquaculture on the sea bass (Dicentrarchus labrax). Anal. Chem. 2005, 77:2587-2594.
    • (2005) Anal. Chem. , vol.77 , pp. 2587-2594
    • Monti, G.1    De Napoli, L.2    Mainolfi, P.3    Barone, R.4    Guida, M.5    Marino, G.6    Amoresano, A.7
  • 20
    • 84871731025 scopus 로고    scopus 로고
    • The sarcoplasmic fish proteome: pathways, metabolic networks and potential bioactive peptides for nutritional inferences
    • Carrera M., Cañas B., Gallardo J.M. The sarcoplasmic fish proteome: pathways, metabolic networks and potential bioactive peptides for nutritional inferences. J. Proteomics 2013, 78:211-220.
    • (2013) J. Proteomics , vol.78 , pp. 211-220
    • Carrera, M.1    Cañas, B.2    Gallardo, J.M.3
  • 21
    • 0032807732 scopus 로고    scopus 로고
    • Characterization of muscle sarcoplasmic and myofibrillar protein hydrolysis caused by Lactobacillus plantarum
    • Fadda S., Sanz Y., Vignolo G., Aristoy M.C., Oliver G., Toldrá F. Characterization of muscle sarcoplasmic and myofibrillar protein hydrolysis caused by Lactobacillus plantarum. Appl. Environ. Microbiol. 1999, 65:3540-3546.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3540-3546
    • Fadda, S.1    Sanz, Y.2    Vignolo, G.3    Aristoy, M.C.4    Oliver, G.5    Toldrá, F.6
  • 22
    • 84942303243 scopus 로고    scopus 로고
    • Development of an analytical strategy for the identification of potential bioactive peptides generated by in vitro tryptic digestion of fish muscle proteins
    • Capriotti A.L., Cavaliere C., Foglia P., Piovesana S., Samperi R., Zenezini Chiozzi R., Laganà A. Development of an analytical strategy for the identification of potential bioactive peptides generated by in vitro tryptic digestion of fish muscle proteins. Anal. Bioanal. Chem. 2015, 407:845-854.
    • (2015) Anal. Bioanal. Chem. , vol.407 , pp. 845-854
    • Capriotti, A.L.1    Cavaliere, C.2    Foglia, P.3    Piovesana, S.4    Samperi, R.5    Zenezini Chiozzi, R.6    Laganà, A.7
  • 23
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D., Flügge U.I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 1984, 138:141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 24
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema P.J., Raijmakers R., Lemeer S., Mohammed S., Heck A.J.R. Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat. Protoc. 2009, 4:484-494.
    • (2009) Nat. Protoc. , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.R.5
  • 25
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J., Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 2008, 26:1367-1372.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 26
    • 73249116888 scopus 로고    scopus 로고
    • Software tool for researching annotations of proteins: open-source protein annotation software with data visualization
    • Bhatia V.N., Perlman D.H., Costello C.E., McComb M.E. Software tool for researching annotations of proteins: open-source protein annotation software with data visualization. Anal. Chem. 2009, 81:9819-9823.
    • (2009) Anal. Chem. , vol.81 , pp. 9819-9823
    • Bhatia, V.N.1    Perlman, D.H.2    Costello, C.E.3    McComb, M.E.4
  • 27
    • 84966475108 scopus 로고    scopus 로고
    • Springer, New York
    • Nielsen S.S. Food Analysis 2010, 275. Springer, New York. fourth ed.
    • (2010) Food Analysis , pp. 275
    • Nielsen, S.S.1
  • 30
    • 84876722167 scopus 로고    scopus 로고
    • Comparative study of label and label-free techniques using shotgun proteomics for relative protein quantification
    • Sjödin M.O.D., Wetterhall M., Kultima K., Artemenko K. Comparative study of label and label-free techniques using shotgun proteomics for relative protein quantification. J. Chromatogr. B 2013, 928:83-92.
    • (2013) J. Chromatogr. B , vol.928 , pp. 83-92
    • Sjödin, M.O.D.1    Wetterhall, M.2    Kultima, K.3    Artemenko, K.4
  • 31
    • 77149143194 scopus 로고    scopus 로고
    • Fish proteome analysis: model organisms and non-sequenced species
    • Forné I., Abián J., Cerdà J. Fish proteome analysis: model organisms and non-sequenced species. Proteomics 2010, 10:858-872.
    • (2010) Proteomics , vol.10 , pp. 858-872
    • Forné, I.1    Abián, J.2    Cerdà, J.3
  • 36
    • 49249092611 scopus 로고    scopus 로고
    • Identification by proteome analysis of muscle proteins in sea bream (Sparus aurata)
    • Schiavone R., Zilli L., Storelli C., Vilella S. Identification by proteome analysis of muscle proteins in sea bream (Sparus aurata). Eur. Food Res. Technol. 2008, 227:1403-1410.
    • (2008) Eur. Food Res. Technol. , vol.227 , pp. 1403-1410
    • Schiavone, R.1    Zilli, L.2    Storelli, C.3    Vilella, S.4
  • 37
    • 0034786119 scopus 로고    scopus 로고
    • An evaluation of the use of two-dimensional gel electrophoresis in proteomics
    • Ong S.E., Pandey A. An evaluation of the use of two-dimensional gel electrophoresis in proteomics. Biomol. Eng. 2001, 18:195-205.
    • (2001) Biomol. Eng. , vol.18 , pp. 195-205
    • Ong, S.E.1    Pandey, A.2
  • 39
    • 84912054408 scopus 로고    scopus 로고
    • Immunological cross-reactivity between four distant parvalbumins-impact on allergen and diagnostics
    • Sharp M.F., Stephen J.N., Kraft L., Weiss T., Kamath S.D., Lopata A.L. Immunological cross-reactivity between four distant parvalbumins-impact on allergen and diagnostics. Mol. Immunol. 2015, 63:437-448.
    • (2015) Mol. Immunol. , vol.63 , pp. 437-448
    • Sharp, M.F.1    Stephen, J.N.2    Kraft, L.3    Weiss, T.4    Kamath, S.D.5    Lopata, A.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.