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Volumn 61, Issue 2, 2002, Pages 199-204

Changes in proteasome activity during postmortem aging of bovine muscle

Author keywords

Meat aging; Muscle proteolysis; Proteasome

Indexed keywords

BOVINE MUSCLES;

EID: 0036313464     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(01)00187-5     Document Type: Article
Times cited : (66)

References (37)
  • 1
    • 0027755811 scopus 로고
    • Quantification of multi-catalytic proteinase complex (Proteasome) activity by ion-exchange chromatography
    • Arbona, J. L., & Koohmaraie, M. (1993). Quantification of multi-catalytic proteinase complex (Proteasome) activity by ion-exchange chromatography. Journal of Animal Science, 71, 3301-3306.
    • (1993) Journal of Animal Science , vol.71 , pp. 3301-3306
    • Arbona, J.L.1    Koohmaraie, M.2
  • 2
    • 0032152137 scopus 로고    scopus 로고
    • Changes in the calpains and calpastatin during postmortem storage of bovine muscle
    • Boehm, M. L., Kendall, T. L., Thompson, V. F., & Goll, D. E. (1998). Changes in the calpains and calpastatin during postmortem storage of bovine muscle. Journal of Animal Science, 76, 2415-2434.
    • (1998) Journal of Animal Science , vol.76 , pp. 2415-2434
    • Boehm, M.L.1    Kendall, T.L.2    Thompson, V.F.3    Goll, D.E.4
  • 4
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies, K. J. A. (2001). Degradation of oxidized proteins by the 20S proteasome. Biochimie, 94, 301-310.
    • (2001) Biochimie , vol.94 , pp. 301-310
    • Davies, K.J.A.1
  • 5
    • 0000410341 scopus 로고
    • Effects of electrical stimulation on post mortem changes in the activities of two Ca2 + dependant neutral proteinases and their inhibitor in beef muscle
    • Ducastaing, A., Valin, C., Schollmeyer, J., & Cross, R. (1985). Effects of electrical stimulation on post mortem changes in the activities of two Ca2 + dependant neutral proteinases and their inhibitor in beef muscle. Meat Science, 15, 193-202.
    • (1985) Meat Science , vol.15 , pp. 193-202
    • Ducastaing, A.1    Valin, C.2    Schollmeyer, J.3    Cross, R.4
  • 7
    • 0001625634 scopus 로고
    • Ultrastructural changes in bovine longissimus muscle during postmortem ageing
    • Gann, G. L., & Merkel, R. A. (1978). Ultrastructural changes in bovine longissimus muscle during postmortem ageing. Meat Science, 2, 129-144.
    • (1978) Meat Science , vol.2 , pp. 129-144
    • Gann, G.L.1    Merkel, R.A.2
  • 8
    • 0033208806 scopus 로고    scopus 로고
    • Effect of calpastatin on degradation of myofibrillar proteins by μ-calpain under postmortem conditions
    • Geesink, G. H., & Koohmaraie, M. (1999). Effect of calpastatin on degradation of myofibrillar proteins by μ-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
  • 10
    • 0034264486 scopus 로고    scopus 로고
    • Ionic strength-induced inactivation of μ-calpain in postmortem muscle
    • Geesink, G. H., & Koohmaraie, M. (2000). Ionic strength-induced inactivation of μ-calpain in postmortem muscle. Journal of Animal Science, 78, 2336-2343.
    • (2000) Journal of Animal Science , vol.78 , pp. 2336-2343
    • Geesink, G.H.1    Koohmaraie, M.2
  • 12
    • 0030141091 scopus 로고    scopus 로고
    • Proteolysis of specific muscle structural proteins by μ-Calpain at low pH and temperature is similar to degradation in postmortem bovine muscle
    • Huff-Lonergan, E., Mitsuhashi, T., Beekman, D. D., Parrish, F. C. jr, Olson, D. G., & Robson, R. M. (1996). Proteolysis of specific muscle structural proteins by μ-Calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. Journal of Animal Science, 74, 993-1008.
    • (1996) Journal of Animal Science , vol.74 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsuhashi, T.2    Beekman, D.D.3    Parrish F.C., Jr.4    Olson, D.G.5    Robson, R.M.6
  • 14
    • 0003079231 scopus 로고
    • The usefulness of muscle color and pH for segregating beef carcasses into tenderness groups
    • Jeremiah, L. E., Tong, A. K. W., & Gibson, L. L. (1991). The usefulness of muscle color and pH for segregating beef carcasses into tenderness groups. Meat Science, 30, 97-101.
    • (1991) Meat Science , vol.30 , pp. 97-101
    • Jeremiah, L.E.1    Tong, A.K.W.2    Gibson, L.L.3
  • 17
    • 0001619142 scopus 로고
    • Inhibition of postmortem tenderization in ovine carcasses through infusion of zinc
    • Koohmaraie, M. (1990). Inhibition of postmortem tenderization in ovine carcasses through infusion of zinc. Journal of Animal Science, 68, 1476-1483.
    • (1990) Journal of Animal Science , vol.68 , pp. 1476-1483
    • Koohmaraie, M.1
  • 18
    • 0027026199 scopus 로고
    • Ovine skeletal muscle multicatalytic proteinase complex (Proteasome): Purification, characterization, and comparison of its effects on myofibrils with μ-Calpains
    • Koohmaraie, M. (1992a). Ovine skeletal muscle multicatalytic proteinase complex (Proteasome): purification, characterization, and comparison of its effects on myofibrils with μ-Calpains. Journal of Animal Science, 70, 3697-3708.
    • (1992) Journal of Animal Science , vol.70 , pp. 3697-3708
    • Koohmaraie, M.1
  • 19
    • 0026591107 scopus 로고
    • 2+ -dependent proteases (calpains) in post mortem proteolysis and meat tenderness
    • 2+ -dependent proteases (calpains) in post mortem proteolysis and meat tenderness. Biochimie, 74, 239-245.
    • (1992) Biochimie , vol.74 , pp. 239-245
    • Koohmaraie, M.1
  • 20
    • 0002514983 scopus 로고
    • Muscle proteinases and meat aging
    • Koohmaraie, M. (1994). Muscle proteinases and meat aging. Meat Science, 36, 93-104.
    • (1994) Meat Science , vol.36 , pp. 93-104
    • Koohmaraie, M.1
  • 21
    • 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, 193-201.
    • (1996) Meat Science , vol.43 , pp. 193-201
    • Koohmaraie, M.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0031286043 scopus 로고    scopus 로고
    • Proteasome from rabbit skeletal muscle: Some properties and effects on muscle proteins
    • Matsuishi, M., & Okitani, A. (1997). Proteasome from rabbit skeletal muscle: some properties and effects on muscle proteins. Meat Science, 45, 451-462.
    • (1997) Meat Science , vol.45 , pp. 451-462
    • Matsuishi, M.1    Okitani, A.2
  • 24
    • 0035545437 scopus 로고    scopus 로고
    • Role of cystein endopeptidase in rabbit meat tenderisation and some related changes
    • Mestres Prates, J. A., Ribeire, A. M., & Dias Correia, A. D. (2001). Role of cystein endopeptidase in rabbit meat tenderisation and some related changes. Meat Science, 57, 283-290.
    • (2001) Meat Science , vol.57 , pp. 283-290
    • Mestres Prates, J.A.1    Ribeire, A.M.2    Dias Correia, A.D.3
  • 25
    • 0028870142 scopus 로고
    • Branched-chain-amino-acid-preferring peptidase activity of the lobster multicatalytic proteinase (proteasome) and the degradation of myofibrillar proteins
    • Mykles, D. L., & Haire, M. F. (1995). Branched-chain-amino-acid-preferring peptidase activity of the lobster multicatalytic proteinase (proteasome) and the degradation of myofibrillar proteins. Biochemical Journal, 306, 285-291.
    • (1995) Biochemical Journal , vol.306 , pp. 285-291
    • Mykles, D.L.1    Haire, M.F.2
  • 26
    • 0032219241 scopus 로고    scopus 로고
    • Purification and properties of rabbit muscle proteasome, and its effect on myofibrillar structure
    • Otsuka, Y., Homma, N., Shiga, K., Ushiki, J., Ikeuchi, Y., & Suzuki, A. (1998). Purification and properties of rabbit muscle proteasome, and its effect on myofibrillar structure. Meat Science, 49, 365-378.
    • (1998) Meat Science , vol.49 , pp. 365-378
    • Otsuka, Y.1    Homma, N.2    Shiga, K.3    Ushiki, J.4    Ikeuchi, Y.5    Suzuki, A.6
  • 28
    • 0033478347 scopus 로고    scopus 로고
    • The effect of proteasome on myofibrillar structures in bovine skeletal muscle
    • Robert, N., Briand, M., Taylor, R. G., & Briand, Y. (1999). The effect of proteasome on myofibrillar structures in bovine skeletal muscle. Meat Science, 51, 149-153.
    • (1999) Meat Science , vol.51 , pp. 149-153
    • Robert, N.1    Briand, M.2    Taylor, R.G.3    Briand, Y.4
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and application
    • USA
    • Towbin, H., Staehlin, T., & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and application. Proceeding of National Academy of Sciences, USA, 76, 4350-4357.
    • (1979) Proceeding of National Academy of Sciences , vol.76 , pp. 4350-4357
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 34
    • 0001952219 scopus 로고
    • Consumer perceptions of texture: The most important quality attribute of meat?
    • A. Ouali, D. Demeyer, & F. J. M. Smulders (Eds.) Utrecht, The Netherlands: ECCEAMST
    • Warkup, C., Marie, S., & Harrington, G. (1995). Consumer perceptions of texture: the most important quality attribute of meat? In: A. Ouali, D. Demeyer, & F. J. M. Smulders (Eds.), Expression of tissue proteinases and regulation of protein degradation as related to meat quality. Utrecht, The Netherlands: ECCEAMST (pp 225-297).
    • (1995) Expression of Tissue Proteinases and Regulation of Protein Degradation as Related to Meat Quality , pp. 225-297
    • Warkup, C.1    Marie, S.2    Harrington, G.3
  • 36
    • 0000558963 scopus 로고
    • Effects of postmortem pH and temperature on bovine muscle structure and meat tenderness
    • Yu, L. P., & Lee, Y. B. (1986). Effects of postmortem pH and temperature on bovine muscle structure and meat tenderness. Journal of Food Science, 51, 774-780.
    • (1986) Journal of Food Science , vol.51 , pp. 774-780
    • Yu, L.P.1    Lee, Y.B.2
  • 37
    • 0030176663 scopus 로고    scopus 로고
    • Predicting variability of ageing and toughness in beef M. Longissimus lumborum et thoracis
    • Zamora, F., Debiton, E. J., Lepetit, J., Lebert, A., Dransfield, E., & Ouali, A. (1996). Predicting variability of ageing and toughness in beef M. Longissimus lumborum et thoracis. Meat Science, 43, 321-333.
    • (1996) Meat Science , vol.43 , pp. 321-333
    • Zamora, F.1    Debiton, E.J.2    Lepetit, J.3    Lebert, A.4    Dransfield, E.5    Ouali, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.