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Volumn 69, Issue 1, 2005, Pages 79-91

Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus

Author keywords

Meat quality; Pig; Proteolysis; Proteome analysis

Indexed keywords

MEAT QUALITY; PIG; PROTEOLYSIS; PROTEOME ANALYSIS;

EID: 5744228466     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2004.06.019     Document Type: Article
Times cited : (165)

References (41)
  • 1
    • 0002204426 scopus 로고
    • An immunological method to assess protein-degradation in postmortem muscle
    • Bandman, E., & Zdanis, D. (1988). An immunological method to assess protein-degradation in postmortem muscle. Meat Science, 22, 1-19.
    • (1988) Meat Science , vol.22 , pp. 1-19
    • Bandman, E.1    Zdanis, D.2
  • 2
    • 45549117556 scopus 로고
    • A review of the relationships of pH with physical aspects of pork quality
    • Bendall, J. R., & Swatland, H. J. (1988). A review of the relationships of pH with physical aspects of pork quality. Meat Science, 24, 85-126.
    • (1988) Meat Science , vol.24 , pp. 85-126
    • Bendall, J.R.1    Swatland, H.J.2
  • 3
    • 0942278684 scopus 로고    scopus 로고
    • Physical changes of signficance of early post mortem water distribution in porcine M. longissimus
    • Bertram, H. C., Schafer, A., Rosenvold, K., & Andersen, H. J. (2004). Physical changes of signficance of early post mortem water distribution in porcine M. longissimus. Meat Science, 66, 915-924.
    • (2004) Meat Science , vol.66 , pp. 915-924
    • Bertram, H.C.1    Schafer, A.2    Rosenvold, K.3    Andersen, H.J.4
  • 4
    • 0035545466 scopus 로고    scopus 로고
    • Effect of rate of pH decline on muscle enzymes activities in two pig lines
    • Claeys, E., De Smet, S., Demeyer, D., Geers, R., & Buys, N. (2001). Effect of rate of pH decline on muscle enzymes activities in two pig lines. Meat Science, 57, 257-263.
    • (2001) Meat Science , vol.57 , pp. 257-263
    • Claeys, E.1    De Smet, S.2    Demeyer, D.3    Geers, R.4    Buys, N.5
  • 5
    • 49049150297 scopus 로고
    • Comparison of methods for measuring sarcomere length in beef semitendinosus muscle
    • Cross, H. R., West, R. L., & Dutson, T. R. (1981). Comparison of methods for measuring sarcomere length in beef semitendinosus muscle. Meat Science, 5, 261-266.
    • (1981) Meat Science , vol.5 , pp. 261-266
    • Cross, H.R.1    West, R.L.2    Dutson, T.R.3
  • 6
    • 0001383470 scopus 로고
    • Optimisation of tenderisation, ageing and tenderness
    • Dransfield, E. (1994). Optimisation of tenderisation, ageing and tenderness. Meat Science, 36, 105-121.
    • (1994) Meat Science , vol.36 , pp. 105-121
    • Dransfield, E.1
  • 7
    • 49149135249 scopus 로고
    • Tenderising in M. Longissimus dorsi of beef, veal, rabbit, lamb and pork
    • Dransfield, E., Jones, R., & Macfie, H. (1980-1981). Tenderising in M. Longissimus dorsi of beef, veal, rabbit, lamb and pork. Meat Science, 5, 193-147.
    • (1980) Meat Science , vol.5 , pp. 193-147
    • Dransfield, E.1    Jones, R.2    Macfie, H.P.3
  • 8
    • 84985294913 scopus 로고
    • Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, western blotting and immunoflurescence microscopy
    • Fritz, J. D., & Greaser, M. L. (1991). Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, western blotting and immunoflurescence microscopy. Journal of Food Science, 56, 607-615.
    • (1991) Journal of Food Science , vol.56 , pp. 607-615
    • Fritz, J.D.1    Greaser, M.L.2
  • 9
    • 0033208806 scopus 로고    scopus 로고
    • Effect of calpastatin on degradation of myofibrillar proteins by micro-calpain under postmortem conditions
    • Geesink, G. H., & Koohmaraie, M. (1999). Effect of calpastatin on degradation of myofibrillar proteins by micro-calpain under postmortem conditions. Journal of Animal Science, 77, 2685-2692.
    • (1999) Journal of Animal Science , vol.77 , pp. 2685-2692
    • Geesink, G.H.1    Koohmaraie, M.2
  • 11
    • 0036613820 scopus 로고    scopus 로고
    • The degradation of myofibrillar proteins in beef and lamb meat using denaturing electrophoresis - An overview
    • Hopkins, D. L., & Thompson, J. M. (2002). The degradation of myofibrillar proteins in beef and lamb meat using denaturing electrophoresis - An overview. Journal of Muscle Foods, 13, 81-102.
    • (2002) Journal of Muscle Foods , vol.13 , pp. 81-102
    • Hopkins, D.L.1    Thompson, J.M.2
  • 12
    • 0035634655 scopus 로고    scopus 로고
    • The interaction between pH and temperature decline early postmortem on the calpain system and objective tenderness in electrically stimulated beef longissimus dorsi muscle
    • Hwang, I. H., & Thompson, J. M. (2001). The interaction between pH and temperature decline early postmortem on the calpain system and objective tenderness in electrically stimulated beef longissimus dorsi muscle. Meat Science, 58, 167-174.
    • (2001) Meat Science , vol.58 , pp. 167-174
    • Hwang, I.H.1    Thompson, J.M.2
  • 13
    • 0038267939 scopus 로고    scopus 로고
    • The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness
    • Hwang, I. H., Devine, C. E., & Hopkins, D. L. (2003). The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness. Meat Science, 65, 677-691.
    • (2003) Meat Science , vol.65 , pp. 677-691
    • Hwang, I.H.1    Devine, C.E.2    Hopkins, D.L.3
  • 14
    • 0037023852 scopus 로고    scopus 로고
    • Review - Proteomic analysis of striated muscle
    • Isfort, R. J. (2002). Review - Proteomic analysis of striated muscle. Journal of Chromatography, 771, 155-165.
    • (2002) Journal of Chromatography , vol.771 , pp. 155-165
    • Isfort, R.J.1
  • 15
    • 0002514983 scopus 로고
    • Muscle proteinases and meat ageing
    • Koohmaraie, M. (1994). Muscle proteinases and meat ageing. Meat Science, 36, 93-104.
    • (1994) Meat Science , vol.36 , pp. 93-104
    • Koohmaraie, M.1
  • 16
    • 0030305245 scopus 로고    scopus 로고
    • Biochemical factors regulating the toughening and tenderization processes of meat
    • Koohmaraie, M. (1996). Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science, 43(Suppl S), S193-S201.
    • (1996) Meat Science , vol.43 , Issue.SUPPL. S
    • Koohmaraie, M.1
  • 17
    • 0035606922 scopus 로고    scopus 로고
    • The effect of ageing on the water-holding capacity of pork: Role of cytoskeletal proteins
    • Kristensen, L., & Purslow, P. P. (2001). The effect of ageing on the water-holding capacity of pork: role of cytoskeletal proteins. Meat Science, 58, 17-23.
    • (2001) Meat Science , vol.58 , pp. 17-23
    • Kristensen, L.1    Purslow, P.P.2
  • 18
    • 0034769635 scopus 로고    scopus 로고
    • Proteome analysis applied to meat science: Characterizing postmortem changes in porcine muscle
    • Lametsch, R., & Bendixen, E. (2001). Proteome analysis applied to meat science: Characterizing postmortem changes in porcine muscle. Journal of Agricultural Food Chemistry, 49, 4531-4537.
    • (2001) Journal of Agricultural Food Chemistry , vol.49 , pp. 4531-4537
    • Lametsch, R.1    Bendixen, E.2
  • 20
    • 0033477445 scopus 로고    scopus 로고
    • Effect of time of deboning and sample size on drip loss of pork
    • Moeseke, W. V., & Smet, S. D. (1999). Effect of time of deboning and sample size on drip loss of pork. Meat Science, 52, 151-156.
    • (1999) Meat Science , vol.52 , pp. 151-156
    • Moeseke, W.V.1    Smet, S.D.2
  • 21
    • 0035609776 scopus 로고    scopus 로고
    • Pork meat quality affects peptide and amino acid profiles during the ageing process
    • Moya, J. J., Flores, M., Aristoy, M. C., & Toldra, F. (2001). Pork meat quality affects peptide and amino acid profiles during the ageing process. Meat Science, 58, 197-206.
    • (2001) Meat Science , vol.58 , pp. 197-206
    • Moya, J.J.1    Flores, M.2    Aristoy, M.C.3    Toldra, F.4
  • 22
    • 0942300430 scopus 로고    scopus 로고
    • N-terminal amino acid sequences of troponin T fragments, including30 kDa one, produced during postmortem aging of bovine longissimus muscle
    • Muroya, S., Kitamura, S., Tanabe, S., Nishimura, T., Nakajima, I., & Chikuni, K. (2004), N-terminal amino acid sequences of troponin T fragments, including30 kDa one, produced during postmortem aging of bovine longissimus muscle. Meat Science, 67, 19-24.
    • (2004) Meat Science , vol.67 , pp. 19-24
    • Muroya, S.1    Kitamura, S.2    Tanabe, S.3    Nishimura, T.4    Nakajima, I.5    Chikuni, K.6
  • 23
    • 0642315427 scopus 로고    scopus 로고
    • Amino acid sequences of multiple fast and slow troponin T isoforms expressed in adult bovine skeletal muscles
    • Muroya, S., Nakajima, I., & Chikuni, K. (2003). Amino acid sequences of multiple fast and slow troponin T isoforms expressed in adult bovine skeletal muscles. Journal of Animal Science, 81, 1185-1192.
    • (2003) Journal of Animal Science , vol.81 , pp. 1185-1192
    • Muroya, S.1    Nakajima, I.2    Chikuni, K.3
  • 24
    • 44949286385 scopus 로고
    • Modelling of the formation of pale, soft and exudative meat: Effects of chilling regime and rate and extent of glycolysis
    • Offer, O. (1991). Modelling of the formation of pale, soft and exudative meat: Effects of chilling regime and rate and extent of glycolysis. Meat Science, 30, 157-184.
    • (1991) Meat Science , vol.30 , pp. 157-184
    • Offer, O.1
  • 25
    • 0000423344 scopus 로고
    • The mechanism of drip production: Formation of two compartments of extracellular space in muscle post mortem
    • Offer, G., & Cousins, T. (1992). The mechanism of drip production: Formation of two compartments of extracellular space in muscle post mortem. Journal of the Science of Food and Agriculture, 58, 107-116.
    • (1992) Journal of the Science of Food and Agriculture , vol.58 , pp. 107-116
    • Offer, G.1    Cousins, T.2
  • 26
    • 0000091348 scopus 로고
    • The structural basis of the water-holding, appearance and toughness of meat and meat products
    • Offer, G., Knight, P., Jeacocke, R., Almond, R., Cousins, T., Elsey, J., et al. (1989). The structural basis of the water-holding, appearance and toughness of meat and meat products. Food Microstructure, 8, 151-170.
    • (1989) Food Microstructure , vol.8 , pp. 151-170
    • Offer, G.1    Knight, P.2    Jeacocke, R.3    Almond, R.4    Cousins, T.5    Elsey, J.6
  • 27
    • 0037208101 scopus 로고    scopus 로고
    • Survey of conditioning indicators for pork loins: Changes in myofibrils, proteins and peptides during postmortem conditioning of vacuum-packed pork loins for 30 days
    • Okumura, T., Yamada, R., & Nishimura, T. (2003). Survey of conditioning indicators for pork loins: changes in myofibrils, proteins and peptides during postmortem conditioning of vacuum-packed pork loins for 30 days. Meat Science, 64, 467-473.
    • (2003) Meat Science , vol.64 , pp. 467-473
    • Okumura, T.1    Yamada, R.2    Nishimura, T.3
  • 28
    • 0001510513 scopus 로고    scopus 로고
    • Relationship of myofibril fragmentation index to measures of beefsteak tenderness
    • Olson, D. G., & Parrish, F. C. (1997). Relationship of myofibril fragmentation index to measures of beefsteak tenderness. Journal of Food Science, 42, 507-509.
    • (1997) Journal of Food Science , vol.42 , pp. 507-509
    • Olson, D.G.1    Parrish, F.C.2
  • 29
    • 0037826704 scopus 로고
    • Scientific basis for electrical stimulation
    • D. H. Pearson, & T. R. Dutson (Eds.). Westport CT: AVI Publishing Company
    • Pearson, A. M., & Dutson, T. R. (1985). Scientific basis for electrical stimulation, In D. H. Pearson, & T. R. Dutson (Eds.). Advances in meat research - Electrical stimulation (Vol. 1, pp. 185-218). Westport CT: AVI Publishing Company.
    • (1985) Advances in Meat Research - Electrical Stimulation , vol.1 , pp. 185-218
    • Pearson, A.M.1    Dutson, T.R.2
  • 31
    • 0036133791 scopus 로고    scopus 로고
    • Tenderness, ageing rate and meat quality of pork M. longissimus thoracis et lumborum after accelerated boning
    • Rees, M. P., Trout, G. R., & Warner, R. D. (2002). Tenderness, ageing rate and meat quality of pork M. longissimus thoracis et lumborum after accelerated boning, Meat Science, 60, 113-124.
    • (2002) Meat Science , vol.60 , pp. 113-124
    • Rees, M.P.1    Trout, G.R.2    Warner, R.D.3
  • 32
    • 0036309401 scopus 로고    scopus 로고
    • Tenderness of pork m. longissimus thoracis et lumborum after accelerated boning. Part I. Effect of temperature conditioning
    • Rees, M. P., Trout, G. R., & Warner, R. D. (2003). Tenderness of pork m. longissimus thoracis et lumborum after accelerated boning. Part I. Effect of temperature conditioning. Meat Science, 61, 205-214.
    • (2003) Meat Science , vol.61 , pp. 205-214
    • Rees, M.P.1    Trout, G.R.2    Warner, R.D.3
  • 33
    • 0037220265 scopus 로고    scopus 로고
    • Factors of significance for pork quality - A review
    • Rosenvold, K., & Andersen, H. J. (2003). Factors of significance for pork quality - a review. Meat Science, 69, 219-237.
    • (2003) Meat Science , vol.69 , pp. 219-237
    • Rosenvold, K.1    Andersen, H.J.2
  • 36
    • 0035257270 scopus 로고    scopus 로고
    • The influence of ultimate pH and intramuscular fat content on pork tenderness and tenderization
    • van Laack, R. L. J. M., Stevens, S. G., & Stalder, K. J. (2001). The influence of ultimate pH and intramuscular fat content on pork tenderness and tenderization. Journal of Animal Science, 79, 392-397.
    • (2001) Journal of Animal Science , vol.79 , pp. 392-397
    • Van Laack, R.L.J.M.1    Stevens, S.G.2    Stalder, K.J.3
  • 37
    • 0031286893 scopus 로고    scopus 로고
    • Muscle protein changes post mortem in relation to pork quality traits
    • Warner, R. D., Kauffman, R. G., & Greaser, M. L. (1997). Muscle protein changes post mortem in relation to pork quality traits. Meat Science, 45, 339-352.
    • (1997) Meat Science , vol.45 , pp. 339-352
    • Warner, R.D.1    Kauffman, R.G.2    Greaser, M.L.3
  • 39
    • 0033195002 scopus 로고    scopus 로고
    • The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major
    • Wheeler, T. D., & Koomaraie, M. (1999). The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major. Journal of Animal Science, 77, 2444-2451.
    • (1999) Journal of Animal Science , vol.77 , pp. 2444-2451
    • Wheeler, T.D.1    Koomaraie, M.2
  • 40
    • 0034331720 scopus 로고    scopus 로고
    • Relationship of beef longissimus tenderness classes to tenderness of gluteus medius, semimembranosus, and biceps femoris
    • Wheeler, T. L., Shackelford, S. D., & Koohmaraie, M. (2000). Relationship of beef longissimus tenderness classes to tenderness of gluteus medius, semimembranosus, and biceps femoris. Journal of Animal Science, 78, 2856-2861.
    • (2000) Journal of Animal Science , vol.78 , pp. 2856-2861
    • Wheeler, T.L.1    Shackelford, S.D.2    Koohmaraie, M.3
  • 41
    • 0035294573 scopus 로고    scopus 로고
    • Separation and identification of rate skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • Yan, J. X., Harry, R. A., Wait, R., Welson, S. Y., Emery, P. W., Preedy, V. R., et al. (2001). Separation and identification of rate skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics, 1, 424-434.
    • (2001) Proteomics , vol.1 , pp. 424-434
    • Yan, J.X.1    Harry, R.A.2    Wait, R.3    Welson, S.Y.4    Emery, P.W.5    Preedy, V.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.