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Volumn 55, Issue 14, 2007, Pages 5834-5841

Comparison of sarcoplasmic proteomes between two groups of pig muscles selected for shear force of cooked meat

Author keywords

Adenylate kinase; Cooked meat; Four and a half LIM domain protein 3; Longissimus lomborum; Pig muscle; Proteome analysis; Warner Bratzler shear force

Indexed keywords

MUSCLE PROTEIN; PROTEOME;

EID: 34447619884     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf070462x     Document Type: Article
Times cited : (64)

References (39)
  • 1
    • 0042858170 scopus 로고    scopus 로고
    • Consumer perceptions: Pork and pig production. Insights from France, England, Sweden and Denmark
    • Ngapo, T. M.; Dransfield, E.; Martin, J. F.; Magnusson, M.; Bredahl, L.; Nute, G. R. Consumer perceptions: pork and pig production. Insights from France, England, Sweden and Denmark. Meat Sci. 2004, 66, 125-134.
    • (2004) Meat Sci , vol.66 , pp. 125-134
    • Ngapo, T.M.1    Dransfield, E.2    Martin, J.F.3    Magnusson, M.4    Bredahl, L.5    Nute, G.R.6
  • 2
    • 0011470221 scopus 로고
    • The relation between rheological properties at small and large deformations and sensory traits of whole meat
    • Josell, A.; Tornberg, E. The relation between rheological properties at small and large deformations and sensory traits of whole meat. Annu. Trans. Nordic Rheol. Soc. 1994, 2, 59-61.
    • (1994) Annu. Trans. Nordic Rheol. Soc , vol.2 , pp. 59-61
    • Josell, A.1    Tornberg, E.2
  • 3
    • 0002103888 scopus 로고    scopus 로고
    • The Eating Quality of Meat
    • Edition, Woodhead Publishing Series in Food Science and Technology; Woodhead: Cambridge, England
    • Lawrie, R. A. The Eating Quality of Meat. In Lawrie's Meat Science. Edition No. 6; Woodhead Publishing Series in Food Science and Technology; Woodhead: Cambridge, England, 1998, p 335.
    • (1998) Lawrie's Meat Science , Issue.6 , pp. 335
    • Lawrie, R.A.1
  • 4
    • 33644509230 scopus 로고    scopus 로고
    • Plastow, G. S.; Carrion, D.; Gil, M.; Garcia-Regueiro, J. A.; Font, I Furnols, M.; Gispert, M.; Olivier, M. A.; Velarde, A.; Guardia, M. D.; Hortos, M.; Rius, M. A.; Sagarra, C.; Diaz, I.; Valero, A.; Sosnicki, A.; Klont, R.; Dornan, S.; Wilkinson, J. M.; Evans, G.; Sargent, C.; Davey, G.; Connolly, D.; Houeix, B.; Maltin, C. M.; Hayes, H. E.; Anandavijayan, V.; Foury, A.; Geverink, N.; Cairns, M.; Tilley, E. E.; Mormède, P.; Blott, S. C. Quality pork genes and meat production. Meat Sci. 2005, 70, 409-421.
    • Plastow, G. S.; Carrion, D.; Gil, M.; Garcia-Regueiro, J. A.; Font, I Furnols, M.; Gispert, M.; Olivier, M. A.; Velarde, A.; Guardia, M. D.; Hortos, M.; Rius, M. A.; Sagarra, C.; Diaz, I.; Valero, A.; Sosnicki, A.; Klont, R.; Dornan, S.; Wilkinson, J. M.; Evans, G.; Sargent, C.; Davey, G.; Connolly, D.; Houeix, B.; Maltin, C. M.; Hayes, H. E.; Anandavijayan, V.; Foury, A.; Geverink, N.; Cairns, M.; Tilley, E. E.; Mormède, P.; Blott, S. C. Quality pork genes and meat production. Meat Sci. 2005, 70, 409-421.
  • 5
    • 0037174398 scopus 로고    scopus 로고
    • Identification of protein degradation during post-mortem storage of pig meat
    • Lametsch, R.; Roepstorff, P.; Bendixen, E. Identification of protein degradation during post-mortem storage of pig meat. J. Agric. Food Chem. 2002, 50, 5508-5512.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 5508-5512
    • Lametsch, R.1    Roepstorff, P.2    Bendixen, E.3
  • 6
    • 1842584567 scopus 로고    scopus 로고
    • Proteome changes during pork meat ageing following use of two different pre-slaughter handling procedures
    • Morzel, M.; Chambon, C.; Hamelin, M.; Santé-Lhoutellier, V.; Sayd, T.; Monin, G. Proteome changes during pork meat ageing following use of two different pre-slaughter handling procedures. Meat Sci. 2004, 67, 689-696.
    • (2004) Meat Sci , vol.67 , pp. 689-696
    • Morzel, M.1    Chambon, C.2    Hamelin, M.3    Santé-Lhoutellier, V.4    Sayd, T.5    Monin, G.6
  • 9
    • 5444224007 scopus 로고    scopus 로고
    • Proteomics approach in meat science: A model study for Hunter L* value and drip loss
    • Hwang, I. Proteomics approach in meat science: a model study for Hunter L* value and drip loss. Food Sci. Biotechnol. 2004, 13, 208-214.
    • (2004) Food Sci. Biotechnol , vol.13 , pp. 208-214
    • Hwang, I.1
  • 11
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of the total lipids from animal tissues
    • Folch, J.; Lee, M.; Sloane Stanley, G. H. A simple method for the isolation and purification of the total lipids from animal tissues. J. Biol. Chem. 1957, 226, 497-509.
    • (1957) J. Biol. Chem , vol.226 , pp. 497-509
    • Folch, J.1    Lee, M.2    Sloane Stanley, G.H.3
  • 12
    • 0004472278 scopus 로고
    • Pork of low technological quality with a normal rate of muscle pH fall in the immediate post-mortem period: The case of the Hampshire breed
    • Monin, G.; Sellier, P. Pork of low technological quality with a normal rate of muscle pH fall in the immediate post-mortem period: The case of the Hampshire breed. Meat Sci. 1985, 13, 49-63.
    • (1985) Meat Sci , vol.13 , pp. 49-63
    • Monin, G.1    Sellier, P.2
  • 15
    • 33646507653 scopus 로고    scopus 로고
    • Modification of trout (Oncorhynchus mykiss) by preslaughter activity
    • Morzel, M.; Chambon, C.; Lefèvre, F.; Paboeuf, G.; Laville, E. Modification of trout (Oncorhynchus mykiss) by preslaughter activity. J Agr. Food Chem. 2006, 54, 2997-3001.
    • (2006) J Agr. Food Chem , vol.54 , pp. 2997-3001
    • Morzel, M.1    Chambon, C.2    Lefèvre, F.3    Paboeuf, G.4    Laville, E.5
  • 16
    • 17444386712 scopus 로고    scopus 로고
    • Data analysis methods for detection of differential protein expression in two-dimensional gel electrophoresis
    • Meunier, B.; Bouley, J.; Piec, I.; Bernard, C.; Picard, B.; Hocquette, J. F. Data analysis methods for detection of differential protein expression in two-dimensional gel electrophoresis. Anal. Biochem. 2005, 340, 226-230.
    • (2005) Anal. Biochem , vol.340 , pp. 226-230
    • Meunier, B.1    Bouley, J.2    Piec, I.3    Bernard, C.4    Picard, B.5    Hocquette, J.F.6
  • 17
    • 0036634367 scopus 로고    scopus 로고
    • New insights into the structure and function of fatty acid-binding proteins
    • Zimmerman, A. W.; Veerkamp, J. H. New insights into the structure and function of fatty acid-binding proteins. CMLS, Cell. Mol., Life Sci. 2002, 59, 1096-1116.
    • (2002) CMLS, Cell. Mol., Life Sci , vol.59 , pp. 1096-1116
    • Zimmerman, A.W.1    Veerkamp, J.H.2
  • 19
    • 18844369302 scopus 로고    scopus 로고
    • Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options
    • Srivastava, S. K.; Ramana, K. V.; Bhatnagar, A. Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Endocrine Rev. 2005, 26 (3), 380-392.
    • (2005) Endocrine Rev , vol.26 , Issue.3 , pp. 380-392
    • Srivastava, S.K.1    Ramana, K.V.2    Bhatnagar, A.3
  • 20
    • 0035087829 scopus 로고    scopus 로고
    • Reduction of ubiquinone by lipoamide dehydrogenase. An antioxidant regenerating pathway
    • Xia, L.; Björnstedt, M.; Nordman, T.; Eriksson, L. C.; Olsson, J. M. Reduction of ubiquinone by lipoamide dehydrogenase. An antioxidant regenerating pathway. Eur. J. Biochem. 2001, 268, 1486-1490.
    • (2001) Eur. J. Biochem , vol.268 , pp. 1486-1490
    • Xia, L.1    Björnstedt, M.2    Nordman, T.3    Eriksson, L.C.4    Olsson, J.M.5
  • 21
    • 0034065158 scopus 로고    scopus 로고
    • The structure and function of initiation factors in eukaryotic protein synthesis
    • Pestova, T. V.; Hellen, C. U. T. The structure and function of initiation factors in eukaryotic protein synthesis. CMLS, Cell. Mol., Life Sci. 2000, 57, 651-674.
    • (2000) CMLS, Cell. Mol., Life Sci , vol.57 , pp. 651-674
    • Pestova, T.V.1    Hellen, C.U.T.2
  • 22
    • 0033133919 scopus 로고    scopus 로고
    • The WD repeat: A common architecture for diverse functions
    • Smith, T. F.; Gaitatzes, C.; Saxena, K.; Neer, E. J. The WD repeat: a common architecture for diverse functions. TIBS 1999, 24, 181-185.
    • (1999) TIBS , vol.24 , pp. 181-185
    • Smith, T.F.1    Gaitatzes, C.2    Saxena, K.3    Neer, E.J.4
  • 23
    • 0035783192 scopus 로고    scopus 로고
    • Review: Cellular substrates of the eukaryotic chaperonin TRIC/CCT
    • Dunn, A. Y.; Melville, M. W.; Frydman, J. Review: cellular substrates of the eukaryotic chaperonin TRIC/CCT. J. Struct. Biol. 2001, 135, 176-184.
    • (2001) J. Struct. Biol , vol.135 , pp. 176-184
    • Dunn, A.Y.1    Melville, M.W.2    Frydman, J.3
  • 24
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • Spiess, C.; Meyer, A. S.; Reissmann, S.; Frydman, J; Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. TRENDS Cell Biol 2004, 14 (11), 598-604.
    • (2004) TRENDS Cell Biol , vol.14 , Issue.11 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 26
    • 0028904661 scopus 로고
    • Distinct biochemichal characteristics of the two human profilin isoforms
    • Gieselmann, R.; Kwiatkowski, D. J.; Janmey, P. A.; Witke, W. Distinct biochemichal characteristics of the two human profilin isoforms. Eur. J. Biochem. 1995, 229, 621-628.
    • (1995) Eur. J. Biochem , vol.229 , pp. 621-628
    • Gieselmann, R.1    Kwiatkowski, D.J.2    Janmey, P.A.3    Witke, W.4
  • 27
    • 0038644934 scopus 로고    scopus 로고
    • Janssen, E.; de Groof, Wijers, M.; Fransen, J.; Dzeja, P. P.; Terzic, A.; Wieringa, B. Adenylate kinase 1 deficiency induces molecular and structural adaptations to support muscle energy metabolism. J. Biol. Biochem. 2003, 278, 12937-12945.
    • Janssen, E.; de Groof, Wijers, M.; Fransen, J.; Dzeja, P. P.; Terzic, A.; Wieringa, B. Adenylate kinase 1 deficiency induces molecular and structural adaptations to support muscle energy metabolism. J. Biol. Biochem. 2003, 278, 12937-12945.
  • 32
    • 33748795108 scopus 로고    scopus 로고
    • Number of intramuscular adipocytes and fatty acid binding protein-4 content are significant indicators of intramuscular fat level in crossbred Large White X Duroc pigs
    • Damon, M.; Louveau, I.; Lefaucheur, L.; Lebret, B.; Vincent, A.; Leroy, P.; Sanchez, M. P.; Herpin, P.; Gondret, F. Number of intramuscular adipocytes and fatty acid binding protein-4 content are significant indicators of intramuscular fat level in crossbred Large White X Duroc pigs. J. Anim. Sci. 2006, 84, 1083-1092.
    • (2006) J. Anim. Sci , vol.84 , pp. 1083-1092
    • Damon, M.1    Louveau, I.2    Lefaucheur, L.3    Lebret, B.4    Vincent, A.5    Leroy, P.6    Sanchez, M.P.7    Herpin, P.8    Gondret, F.9
  • 33
    • 17644401370 scopus 로고    scopus 로고
    • Wang, Y. H.; Byrne, K. A.; Reverter, A.; Harper, G. S.; Taniguchi, McWilliam, S. M.; Mannen, H.; Oyama, K.; Lehnert, S. A. Transcriptional profiling of skeletal muscle tissue from two breeds of cattle. Mamm. Genome 2005, 16, 201-210.
    • Wang, Y. H.; Byrne, K. A.; Reverter, A.; Harper, G. S.; Taniguchi, McWilliam, S. M.; Mannen, H.; Oyama, K.; Lehnert, S. A. Transcriptional profiling of skeletal muscle tissue from two breeds of cattle. Mamm. Genome 2005, 16, 201-210.
  • 34
    • 38149144094 scopus 로고
    • Intramuscular fat and muscle fibre lipid contents in halothane-gene-free pigs fed high or low protein diets and its relation to meat quality
    • Essen-Gustavsson, B.; Karlson, A.; Lundström, K.; Enfält, A. -C. Intramuscular fat and muscle fibre lipid contents in halothane-gene-free pigs fed high or low protein diets and its relation to meat quality. Meat Sci. 1994, 38, 269-277.
    • (1994) Meat Sci , vol.38 , pp. 269-277
    • Essen-Gustavsson, B.1    Karlson, A.2    Lundström, K.3    Enfält, A.-C.4
  • 35
    • 0002459255 scopus 로고    scopus 로고
    • Comparison of intramuscular adipose tissue cellularity in muscles differing in their lipid content and fibre type composition during rabbit growth
    • Gondret, F.; Mourot, J.; Bonneau, M. Comparison of intramuscular adipose tissue cellularity in muscles differing in their lipid content and fibre type composition during rabbit growth. Livest. Prod. Sci. 1998, 54, 1-10.
    • (1998) Livest. Prod. Sci , vol.54 , pp. 1-10
    • Gondret, F.1    Mourot, J.2    Bonneau, M.3
  • 36
    • 0033729385 scopus 로고    scopus 로고
    • Lipid-binding proteins modulate ligand-dependant transactivation by by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm
    • Helledie, T.; Antonius, M.; Sorensen, R. V.; Hertzel, A. V.; Bernlohr, D. A.; Kolvraa, S.; Kristiansen, K.; Mandrup, S. Lipid-binding proteins modulate ligand-dependant transactivation by by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000, 41, 1740-1751.
    • (2000) J. Lipid Res , vol.41 , pp. 1740-1751
    • Helledie, T.1    Antonius, M.2    Sorensen, R.V.3    Hertzel, A.V.4    Bernlohr, D.A.5    Kolvraa, S.6    Kristiansen, K.7    Mandrup, S.8
  • 38
    • 34447635634 scopus 로고
    • The effect of fatness on some processing and palatability characteristics of pork carcasses
    • Saffle, R. L.; Bratzler, L. J. The effect of fatness on some processing and palatability characteristics of pork carcasses. Food Technol. 1959, 13, 236-241.
    • (1959) Food Technol , vol.13 , pp. 236-241
    • Saffle, R.L.1    Bratzler, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.