메뉴 건너뛰기




Volumn 66, Issue 2, 2004, Pages 317-327

Does the newly discovered calpain 10 play a role in meat tenderization during post-mortem storage?

Author keywords

Calpain 10; Desmin; Skeletal muscle; Tenderness

Indexed keywords

ENZYMES; MUSCLE; PROTEINS;

EID: 0142200878     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(03)00106-2     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 0032152137 scopus 로고    scopus 로고
    • Changes in the calpains and calpastatin during post-mortem storage of bovine muscle
    • Boehm, M. L., Kendall, T. L., Thompson, V. F., & Goll, D. E. (1998). Changes in the calpains and calpastatin during post-mortem 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
  • 2
    • 0011411614 scopus 로고
    • Publication No. 872. Hamilton: Meat Industries Research Institute of New Zealand
    • Chrystall, B. B., & Devine, N. (1991). Quality assurance for tenderness (Publication No. 872). Hamilton: Meat Industries Research Institute of New Zealand.
    • (1991) Quality Assurance for Tenderness
    • Chrystall, B.B.1    Devine, N.2
  • 3
    • 0032722011 scopus 로고    scopus 로고
    • Diverse mRNA expression patterns of the mouse calpain genes Capn5, Capn6 and Capn11 during development
    • Dear, T. N., & Boehm, T. (1999). Diverse mRNA expression patterns of the mouse calpain genes Capn5, Capn6 and Capn11 during development. Mechanisms of Development, 89, 201-209.
    • (1999) Mechanisms of Development , vol.89 , pp. 201-209
    • Dear, T.N.1    Boehm, T.2
  • 4
    • 0031259933 scopus 로고    scopus 로고
    • A new subfamily of vertebrate calpains lacking a calmodulin-like domain: Implications for calpain regulation and evolution
    • Dear, T. N., Matena, K., Vingron, M., & Boehm, T. (1997). A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution. Genomics, 45, 175-184.
    • (1997) Genomics , vol.45 , pp. 175-184
    • Dear, T.N.1    Matena, K.2    Vingron, M.3    Boehm, T.4
  • 5
    • 0034283590 scopus 로고    scopus 로고
    • Gene structure, chromosomal localisation, and expression pattern of capn 12, a new member of the calpain large subunit gene family
    • Dear, T. N., Meier, N. T., Hunn, M., & Boehm, T. (2000). Gene structure, chromosomal localisation, and expression pattern of capn 12, a new member of the calpain large subunit gene family. Genomics, 68, 152-160.
    • (2000) Genomics , vol.68 , pp. 152-160
    • Dear, T.N.1    Meier, N.T.2    Hunn, M.3    Boehm, T.4
  • 6
    • 0032801290 scopus 로고    scopus 로고
    • Capn7: A highly divergent vertebrate calpain with a novel C-terminal domain
    • Franz, T., Vingron, M., Boehm, T., & Dear, T. N. (1999). Capn7: a highly divergent vertebrate calpain with a novel C-terminal domain. Mammalian Genome, 10, 318-321.
    • (1999) Mammalian Genome , vol.10 , pp. 318-321
    • Franz, T.1    Vingron, M.2    Boehm, T.3    Dear, T.N.4
  • 9
    • 0036198178 scopus 로고    scopus 로고
    • Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderization in beef and sheep meat
    • Hopkins, D. L., & Thompson, J. M. (2002). Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderization in beef and sheep meat. Australian Journal of Agricultural Research, 53, 149-166.
    • (2002) Australian Journal of Agricultural Research , vol.53 , pp. 149-166
    • Hopkins, D.L.1    Thompson, J.M.2
  • 11
    • 0030141091 scopus 로고    scopus 로고
    • Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in post-mortem 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 post-mortem 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
    • 85030955997 scopus 로고    scopus 로고
    • The relationship between meat tenderization, myofibrillar fragmentation and autolysis of calpain 3 during post-mortem aging
    • in press
    • Ilian, M. A., Bekhit, A., & Bickerstaffe, R. The relationship between meat tenderization, myofibrillar fragmentation and autolysis of calpain 3 during post-mortem aging. Meat Science (in press).
    • Meat Science
    • Ilian, M.A.1    Bekhit, A.2    Bickerstaffe, R.3
  • 15
    • 0032528020 scopus 로고    scopus 로고
    • SOLH, a human homologue of the Drosophila melanogaster small optic lobes gene is a member of the calpain and zinc-finger gene families and maps to human chromosome 16p 13.3 near CATM (cataract with microphthalmia)
    • Kamei, M., Webb, G. C., Young, I. G., & Campbell, H. D. (1998). SOLH, a human homologue of the Drosophila melanogaster small optic lobes gene is a member of the calpain and zinc-finger gene families and maps to human chromosome 16p 13.3 near CATM (cataract with microphthalmia). Genomics, 51, 197-206.
    • (1998) Genomics , vol.51 , pp. 197-206
    • Kamei, M.1    Webb, G.C.2    Young, I.G.3    Campbell, H.D.4
  • 18
    • 0026591107 scopus 로고
    • The role of Ca(2 +)-dependent proteases (calpains) in post-mortem proteolysis and meat tenderness
    • Koohmaraie, M. (1992). The role of Ca(2 +)-dependent proteases (calpains) in post-mortem proteolysis and meat tenderness. Biochimie, 74, 39-45.
    • (1992) Biochimie , vol.74 , pp. 39-45
    • Koohmaraie, M.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0031755539 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system
    • Masumoto, H., Yoshizawa, T., Sorimachi, H., Nishino, T., Ishiura, S., & Suzuki, K. (1998). Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system. Journal of Bochemistry, 124, 957-961.
    • (1998) Journal of Bochemistry , vol.124 , pp. 957-961
    • Masumoto, H.1    Yoshizawa, T.2    Sorimachi, H.3    Nishino, T.4    Ishiura, S.5    Suzuki, K.6
  • 22
    • 78651537306 scopus 로고
    • Integration and control of metabolic processes
    • Redwood City, California, USA: The Benjamin/Cummings Publishing Company, Inc.
    • Mathews, C. K., & van Holde, K. E. (1990). Integration and control of metabolic processes. In Biochemistry (pp. 782). Redwood City, California, USA: The Benjamin/Cummings Publishing Company, Inc.
    • (1990) Biochemistry , pp. 782
    • Mathews, C.K.1    Van Holde, K.E.2
  • 23
    • 0028171412 scopus 로고
    • 2--activiated neutral protease is active in the erythrocyte membrane in its nonautolyzed 80-kDa form
    • 2--activiated neutral protease is active in the erythrocyte membrane in its nonautolyzed 80-kDa form. Journal of Biological Chemistry, 269, 27992-27995.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 27992-27995
    • Molinari, M.1    Anagli, J.2    Carafoli, E.3
  • 24
    • 0035200353 scopus 로고    scopus 로고
    • Dissociation of m-calpain subunits occurs after autolysis of the N-terminus of the catalytic subunit, and is not required for activation
    • Nakagawa, K., Masumoto, H., Sorimachi, H., & Suzuki, K. (2001). Dissociation of m-calpain subunits occurs after autolysis of the N-terminus of the catalytic subunit, and is not required for activation. Journal of Biochemistry, 130, 605-611.
    • (2001) Journal of Biochemistry , vol.130 , pp. 605-611
    • Nakagawa, K.1    Masumoto, H.2    Sorimachi, H.3    Suzuki, K.4
  • 29
    • 0036453977 scopus 로고    scopus 로고
    • Contribution of ubiquitous calpains to cataractogenesis in the spontaneous diabetic WBN/Kob rat
    • Sakamoto-Mizutani, K., Fukiage, C., Tamada, Y., Azuma, M., & Shearer, T. (2002). Contribution of ubiquitous calpains to cataractogenesis in the spontaneous diabetic WBN/Kob rat. Experimental Eye research, 75, 611-617.
    • (2002) Experimental Eye Research , vol.75 , pp. 611-617
    • Sakamoto-Mizutani, K.1    Fukiage, C.2    Tamada, Y.3    Azuma, M.4    Shearer, T.5
  • 31
    • 0023154182 scopus 로고
    • Calcium activated neutral protease: Domain structure and activity regulation
    • Suzuki, K. (1987). Calcium activated neutral protease: domain structure and activity regulation. Trends in Biochemical Science, 12, 103-105.
    • (1987) Trends in Biochemical Science , vol.12 , pp. 103-105
    • Suzuki, K.1
  • 35
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staedhin, T., & Gordon, J. (1979). Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences (USA), 76, 4350-4354.
    • (1979) Proceedings of the National Academy of Sciences (USA) , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staedhin, T.2    Gordon, J.3
  • 36
    • 0035381015 scopus 로고    scopus 로고
    • Effect of post-mortem storage on μ-calpain and m-calpain in ovine skeletal muscle
    • Veiseth, E., Shackelford, S. D., Wheeler, T. L., & Koohmaraie, M. (2001). Effect of post-mortem storage on μ-calpain and m-calpain in ovine skeletal muscle. Journal of Animal Science, 79, 1502-1508.
    • (2001) Journal of Animal Science , vol.79 , pp. 1502-1508
    • Veiseth, E.1    Shackelford, S.D.2    Wheeler, T.L.3    Koohmaraie, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.