메뉴 건너뛰기




Volumn 76, Issue 9, 1998, Pages 2415-2434

Changes in the Calpains and Calpastatin During Postmortem Storage of Bovine Muscle

Author keywords

Aging; Bovidae; Calpain; Calpastatin; Meat Characteristics; Postmortem Changes

Indexed keywords

BOVIDAE; BOVINAE;

EID: 0032152137     PISSN: 00218812     EISSN: None     Source Type: Journal    
DOI: 10.2527/1998.7692415x     Document Type: Article
Times cited : (155)

References (74)
  • 1
    • 0025751548 scopus 로고
    • Desmin is present in proliferating rat muscle satellite cells but not in bovine muscle satellite cells
    • Allen, R. E., L. L. Rankin, E. A. Greene, L. K. Boxhorn, P. R. Pierce, and S. E. Johnson. 1991. Desmin is present in proliferating rat muscle satellite cells but not in bovine muscle satellite cells. J. Cell. Physiol. 149:525-535.
    • (1991) J. Cell. Physiol. , vol.149 , pp. 525-535
    • Allen, R.E.1    Rankin, L.L.2    Greene, E.A.3    Boxhorn, L.K.4    Pierce, P.R.5    Johnson, S.E.6
  • 2
    • 84985297641 scopus 로고
    • Postmortem degradation of titin and nebulin of beef steaks varying in tenderness
    • Anderson, T. J., and F. C. Parrish, Jr. 1989. Postmortem degradation of titin and nebulin of beef steaks varying in tenderness. J. Food Sci. 54:748-749.
    • (1989) J. Food Sci. , vol.54 , pp. 748-749
    • Anderson, T.J.1    Parrish F.C., Jr.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0017101439 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle. Biochemistry 15:2150-2158.
    • (1976) Biochemistry , vol.15 , pp. 2150-2158
    • Dayton, W.R.1    Goll, D.E.2    Zeece, M.G.3    Robson, R.M.4    Reville, W.J.5
  • 8
    • 0002741564 scopus 로고
    • Modelling post-mortem tenderization-III: Role of calpain in conditioning
    • Dransfield, E. 1992. Modelling post-mortem tenderization-III: Role of calpain in conditioning. Meat Sci. 31:85-94.
    • (1992) Meat Sci. , vol.31 , pp. 85-94
    • Dransfield, E.1
  • 10
    • 0026073804 scopus 로고
    • Comparison of the autolyzed and unautolyzed forms of μ- and m-calpain from bovine skeletal muscle
    • Edmunds, T., P. A. Nagainis, S. K. Sathe, V. F. Thompson, and D. E. Goll. 1991. Comparison of the autolyzed and unautolyzed forms of μ- and m-calpain from bovine skeletal muscle. Biochim. Biophys. Acta 1077:197-208.
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 197-208
    • Edmunds, T.1    Nagainis, P.A.2    Sathe, S.K.3    Thompson, V.F.4    Goll, D.E.5
  • 11
    • 0023835174 scopus 로고
    • All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli
    • Emori, Y., H. Kawasaki, S. Imajoh, Y. Minami, and K. Suzuki. 1988. All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli. J. Biol. Chem. 263:2364-2370.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2364-2370
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Minami, Y.4    Suzuki, K.5
  • 12
    • 0001906486 scopus 로고
    • Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin L, calpain I, calpain II, and β-glucuronidase
    • Etherington, D. J., M.A.J. Taylor, and E. Dransfield. 1987. Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin L, calpain I, calpain II, and β-glucuronidase. Meat Sci. 20:1-18.
    • (1987) Meat Sci. , vol.20 , pp. 1-18
    • Etherington, D.J.1    Taylor, M.A.J.2    Dransfield, E.3
  • 13
    • 84985294913 scopus 로고
    • Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, western blotting, and immunofluorescence microscopy
    • Fritz, J. D., and M. L. Greaser. 1991. Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, western blotting, and immunofluorescence microscopy. J. Food Sci. 56:607-615.
    • (1991) J. Food Sci. , vol.56 , pp. 607-615
    • Fritz, J.D.1    Greaser, M.L.2
  • 14
    • 0024402489 scopus 로고
    • Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins
    • Fritz, J. D., D. R. Swartz, and M. L. Greaser. 1989. Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins. Anal. Biochem. 180: 205-210.
    • (1989) Anal. Biochem. , vol.180 , pp. 205-210
    • Fritz, J.D.1    Swartz, D.R.2    Greaser, M.L.3
  • 15
    • 0002318295 scopus 로고
    • Measurements of calpain activity in postmortem muscle extracts underestimates levels of μ-calpain
    • American Meat Science Assoc., Chicago, IL
    • Geesink, G. H., and D. E. Goll. 1995. Measurements of calpain activity in postmortem muscle extracts underestimates levels of μ-calpain. Proc. 41st Annu. Int. Congr. Meat Sci. Technol. pp 547-549. American Meat Science Assoc., Chicago, IL.
    • (1995) Proc. 41st Annu. Int. Congr. Meat Sci. Technol. , pp. 547-549
    • Geesink, G.H.1    Goll, D.E.2
  • 16
    • 0000666240 scopus 로고
    • Postmortem changes in physical and chemical properties of bovine muscle
    • Goll, D. E., D. W. Henderson, and E. A. Kline. 1964. Postmortem changes in physical and chemical properties of bovine muscle. J. Food Sci. 29:590-596.
    • (1964) J. Food Sci. , vol.29 , pp. 590-596
    • Goll, D.E.1    Henderson, D.W.2    Kline, E.A.3
  • 19
    • 0011951174 scopus 로고
    • Extraction, purification, and localization of α-actinin from asynchronous insect flight muscle
    • R. T. Tregcar (Ed.) North-Holland Publishing Co., Amsterdam, The Netherlands
    • Goll, D. E., M. H. Stromer, R. M. Robson, B. M. Luke, and K. S. Hammond. 1977. Extraction, purification, and localization of α-actinin from asynchronous insect flight muscle. In: R. T. Tregcar (Ed.) Insect Flight Muscle. Proc. Oxford Symp. pp 15-40. North-Holland Publishing Co., Amsterdam, The Netherlands.
    • (1977) Insect Flight Muscle. Proc. Oxford Symp. , pp. 15-40
    • Goll, D.E.1    Stromer, M.H.2    Robson, R.M.3    Luke, B.M.4    Hammond, K.S.5
  • 20
    • 0003134522 scopus 로고
    • Role of proteinases and protein turnover in muscle growth and meat quality
    • National Live Stock and Meat Board, Chicago, IL
    • Goll, D. E., R. G. Taylor, J. A. Christiansen, and V. F. Thompson. 1992a. Role of proteinases and protein turnover in muscle growth and meat quality. Proc. 44th Annu. Recip. Meat Conf. pp 25-36. National Live Stock and Meat Board, Chicago, IL.
    • (1992) Proc. 44th Annu. Recip. Meat Conf. , pp. 25-36
    • Goll, D.E.1    Taylor, R.G.2    Christiansen, J.A.3    Thompson, V.F.4
  • 23
    • 0026911137 scopus 로고
    • Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?
    • Goll, D. E., V. F. Thompson, R. G. Taylor, and T. Zalewska. 1992c. Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? Bioessays 14:549-556.
    • (1992) Bioessays , vol.14 , pp. 549-556
    • Goll, D.E.1    Thompson, V.F.2    Taylor, R.G.3    Zalewska, T.4
  • 24
    • 0001741477 scopus 로고
    • Separation of subcellular organelles by differential and density gradient centrifugation
    • National Live Stock and Meat Board, Chicago, IL
    • Goll, D. E., R. B. Young, and M. H. Stromer. 1974b. Separation of subcellular organelles by differential and density gradient centrifugation. Proc. 27th Annu. Recip. Meat Conf. pp 250-290. National Live Stock and Meat Board, Chicago, IL.
    • (1974) Proc. 27th Annu. Recip. Meat Conf. , pp. 250-290
    • Goll, D.E.1    Young, R.B.2    Stromer, M.H.3
  • 25
    • 0021806014 scopus 로고
    • Quantitation of tissue calpain activity after isolation by hydrophobic chromatography
    • Gopalakrishna, R., and S. K. Barsky. 1985. Quantitation of tissue calpain activity after isolation by hydrophobic chromatography. Anal. Biochem. 148:413-423.
    • (1985) Anal. Biochem. , vol.148 , pp. 413-423
    • Gopalakrishna, R.1    Barsky, S.K.2
  • 26
    • 0022973319 scopus 로고
    • Hydrophobic association of calpains with subcellular organelles. Compartmentalization of calpain and the endogenous inhibitor calpastatin in tissues
    • Gopalakrishna, R., and S. K. Barksy. 1986. Hydrophobic association of calpains with subcellular organelles. Compartmentalization of calpain and the endogenous inhibitor calpastatin in tissues. J. Biol. Chem. 261:13936-13942.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13936-13942
    • Gopalakrishna, R.1    Barksy, S.K.2
  • 27
    • 0021824059 scopus 로고
    • Rapid purification of calcium-activated protease by calcium-dependent hydrophobic-interaction chromatography
    • Gopalakrishna, R., and J. F. Head. 1985. Rapid purification of calcium-activated protease by calcium-dependent hydrophobic-interaction chromatography. FEBS Lett. 186:246-250.
    • (1985) FEBS Lett. , vol.186 , pp. 246-250
    • Gopalakrishna, R.1    Head, J.F.2
  • 28
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall, A. G., C. J. Bardawill, and M. M. David. 1949. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177:751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 29
    • 0021153768 scopus 로고
    • Evidence for membrane-associated calpain I in human erythrocytes. Detection by an immunoelectrophoretic blotting method using monospecific antibody
    • Hatanaka, M., N. Yoshimura, T. Murakami, R. Kannagi, and T. Muracki. 1984. Evidence for membrane-associated calpain I in human erythrocytes. Detection by an immunoelectrophoretic blotting method using monospecific antibody. Biochemistry 23: 3272-3276.
    • (1984) Biochemistry , vol.23 , pp. 3272-3276
    • Hatanaka, M.1    Yoshimura, N.2    Murakami, T.3    Kannagi, R.4    Muracki, T.5
  • 30
    • 0028126638 scopus 로고
    • Identification of the 30-kDa polypeptide in postmortem skeletal muscle as a degradation product of troponin-T
    • Ho, C.-Y., M. H. Stromer, and R. M. Robson. 1994. Identification of the 30-kDa polypeptide in postmortem skeletal muscle as a degradation product of troponin-T. Biochimie 76:369-375.
    • (1994) Biochimie , vol.76 , pp. 369-375
    • Ho, C.-Y.1    Stromer, M.H.2    Robson, R.M.3
  • 31
    • 0030183591 scopus 로고    scopus 로고
    • Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle
    • Ho, C.-Y., M. H. Stromer, and R. M. Robson. 1996. Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle. J. Anim. Sci. 74:1563-1575.
    • (1996) J. Anim. Sci. , vol.74 , pp. 1563-1575
    • Ho, C.-Y.1    Stromer, M.H.2    Robson, R.M.3
  • 32
    • 0031068543 scopus 로고    scopus 로고
    • Effects of electrical stimulation and postmortem storage on changes in titin, nebulin, desmin, troponin-T, and muscle ultrastructure in Bos indicus crossbred cattle
    • Ho, C.-Y., M. H. Stromer, G. Rouse, and R. M. Robson. 1997. Effects of electrical stimulation and postmortem storage on changes in titin, nebulin, desmin, troponin-T, and muscle ultrastructure in Bos indicus crossbred cattle. J. Anim. Sci. 75:366-376.
    • (1997) J. Anim. Sci. , vol.75 , pp. 366-376
    • Ho, C.-Y.1    Stromer, M.H.2    Rouse, G.3    Robson, R.M.4
  • 33
    • 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., T. Mitsubishi, D. D. Beekman, F. C. Parrish, Jr., D. G. Olson, and R. M. Robson. 1996. Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J. Anim. Sci. 74:993-1008.
    • (1996) J. Anim. Sci. , vol.74 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsubishi, T.2    Beekman, D.D.3    Parrish F.C., Jr.4    Olson, D.G.5    Robson, R.M.6
  • 34
    • 0029285632 scopus 로고
    • Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle
    • Huff-Lonergan, E., F. C. Parrish, Jr., and R. M. Robson. 1995. Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle. J. Anim. Sci. 73:1064-1073.
    • (1995) J. Anim. Sci. , vol.73 , pp. 1064-1073
    • Huff-Lonergan, E.1    Parrish F.C., Jr.2    Robson, R.M.3
  • 35
    • 84987369453 scopus 로고
    • Studies of desmin and α-actinin degradation in bovine semitendinosus muscle
    • Hwan, S. F., and E. Bandman. 1989. Studies of desmin and α-actinin degradation in bovine semitendinosus muscle. J. Food Sci. 54:1426-1430.
    • (1989) J. Food Sci. , vol.54 , pp. 1426-1430
    • Hwan, S.F.1    Bandman, E.2
  • 36
    • 43949173699 scopus 로고
    • The concentrations of free magnesium and free calcium ions both increase in skeletal muscle fibers entering rigor mortis
    • Jeacocke, R. 1993. The concentrations of free magnesium and free calcium ions both increase in skeletal muscle fibers entering rigor mortis. Meat Sci. 35:27-45.
    • (1993) Meat Sci. , vol.35 , pp. 27-45
    • Jeacocke, R.1
  • 37
    • 0022373682 scopus 로고
    • A simple one-step procedure for the separation of calpain I, calpain II, and calpastatin
    • Karlsson, J.-O., S. Gustavsson, C. Hall, and E. Nilsson. 1985. A simple one-step procedure for the separation of calpain I, calpain II, and calpastatin. Biochem. J. 231:201-204.
    • (1985) Biochem. J. , vol.231 , pp. 201-204
    • Karlsson, J.-O.1    Gustavsson, S.2    Hall, C.3    Nilsson, E.4
  • 38
    • 0002526577 scopus 로고
    • The role of endogenous proteases in meat tenderness
    • National Live Stock and Meat Board. Chicago, IL
    • Koohmaraie, M. 1988. The role of endogenous proteases in meat tenderness. Proc. 41st Annu. Recip. Meat Conf. pp 89-100. National Live Stock and Meat Board. Chicago, IL.
    • (1988) Proc. 41st Annu. Recip. Meat Conf. , pp. 89-100
    • Koohmaraie, M.1
  • 39
    • 0025392636 scopus 로고
    • 2+-dependent protease activities by hydrophobic and ion-exchange chromatography
    • 2+-dependent protease activities by hydrophobic and ion-exchange chromatography. J. Anim. Sci. 68:659-665.
    • (1990) J. Anim. Sci. , vol.68 , pp. 659-665
    • Koohmaraie, M.1
  • 40
    • 0026591107 scopus 로고
    • 2+-dependent proteinases (calpains) in post-mortem proteolysis and meat tenderness
    • 2+-dependent proteinases (calpains) in post-mortem proteolysis and meat tenderness. Biochimie 74:239-245.
    • (1992) Biochimie , vol.74 , pp. 239-245
    • Koohmaraie, M.1
  • 41
    • 84985208668 scopus 로고
    • 2+-dependent proteases and lysosomal enzymes in postmortem changes in bovine skeletal muscle
    • 2+-dependent proteases and lysosomal enzymes in postmortem changes in bovine skeletal muscle. J. Food Sci. 53:1253-1257.
    • (1988) J. Food Sci. , vol.53 , pp. 1253-1257
    • Koohmaraie, M.1    Babiker, A.S.2    Merkel, R.A.3    Dutson, T.R.4
  • 42
    • 0024653898 scopus 로고
    • Acceleration of postmortem tenderization in ovine carcasses through infusion of calcium chloride: Effect of concentration and ionic strength
    • Koohmaraie, M., J. D. Crouse, and H. J. Mersmann. 1989. Acceleration of postmortem tenderization in ovine carcasses through infusion of calcium chloride: Effect of concentration and ionic strength. J. Anim. Sci. 67:934-942.
    • (1989) J. Anim. Sci. , vol.67 , pp. 934-942
    • Koohmaraie, M.1    Crouse, J.D.2    Mersmann, H.J.3
  • 43
    • 0030330032 scopus 로고    scopus 로고
    • Meat toughening does not occur when rigor shortening is prevented
    • Koohmaraie, M., M. E. Doumit, and T. L. Wheeler. 1996a. Meat toughening does not occur when rigor shortening is prevented. J. Anim. Sci. 74:2935-2942.
    • (1996) J. Anim. Sci. , vol.74 , pp. 2935-2942
    • Koohmaraie, M.1    Doumit, M.E.2    Wheeler, T.L.3
  • 45
    • 0002451154 scopus 로고
    • Effect of low-calcium-requiring calcium activated factor on myofibrils under varying pH and temperature conditions
    • Koohmaraie, M., J. E. Schollmeyer, and T. R. Dutson. 1986. Effect of low-calcium-requiring calcium activated factor on myofibrils under varying pH and temperature conditions. J. Food Sci. 51: 28-32+.
    • (1986) J. Food Sci. , vol.51
    • Koohmaraie, M.1    Schollmeyer, J.E.2    Dutson, T.R.3
  • 48
    • 0029685798 scopus 로고    scopus 로고
    • Effects of a β-adrenergic agonist (L-644,969) and male sex condition on muscle growth and meat quality of callipyge lambs
    • Koohmaraie, M., S. D. Shackelford, and T. L. Wheeler. 1996b. Effects of a β-adrenergic agonist (L-644,969) and male sex condition on muscle growth and meat quality of callipyge lambs. J. Anim. Sci. 74:70-79.
    • (1996) J. Anim. Sci. , vol.74 , pp. 70-79
    • Koohmaraie, M.1    Shackelford, S.D.2    Wheeler, T.L.3
  • 49
    • 0029443229 scopus 로고
    • A muscle hypertrophy condition in lamb (callipyge): Characterization of effects on muscle growth and meat quality traits
    • Koohmaraie, M., S. D. Shackelford, T. L. Wheeler, S. M. Lonergan, and M. E. Doumit. 1995b. A muscle hypertrophy condition in lamb (callipyge): Characterization of effects on muscle growth and meat quality traits. J. Anim. Sci. 73:3596-3607.
    • (1995) J. Anim. Sci. , vol.73 , pp. 3596-3607
    • Koohmaraie, M.1    Shackelford, S.D.2    Wheeler, T.L.3    Lonergan, S.M.4    Doumit, M.E.5
  • 50
    • 0024452933 scopus 로고
    • In vivo effect of a β-adrenergic agonist on activity of calcium-dependent proteinases, their specific inhibitor, and cathepsins B and H in skeletal muscle
    • Kretchmar, D. H., M. R. Hathaway, R. J. Epley, and W. R. Dayton. 1989. In vivo effect of a β-adrenergic agonist on activity of calcium-dependent proteinases, their specific inhibitor, and cathepsins B and H in skeletal muscle. Arch. Biochem. Biophys. 275:228-235.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 228-235
    • Kretchmar, D.H.1    Hathaway, M.R.2    Epley, R.J.3    Dayton, W.R.4
  • 51
    • 0026515545 scopus 로고
    • Multiple forms of rat calpastatin cDNA in the coding region of functionally unknown amino-terminal domain
    • Lee, W. J., M. Hatanaka, and M. Maki. 1992a. Multiple forms of rat calpastatin cDNA in the coding region of functionally unknown amino-terminal domain. Biochim. Biophys. Acta 1129:251-253.
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 251-253
    • Lee, W.J.1    Hatanaka, M.2    Maki, M.3
  • 52
    • 0026644784 scopus 로고
    • Molecular diversity in the amino-terminal domains of human calpastatin by exon skipping
    • Lee, W. J., H. Ma, E. Takano, H. Q. Yang, M. Hatanaka, and M. Maki. 1992b. Molecular diversity in the amino-terminal domains of human calpastatin by exon skipping. J. Biol. Chem. 267:8437-8442.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8437-8442
    • Lee, W.J.1    Ma, H.2    Takano, E.3    Yang, H.Q.4    Hatanaka, M.5    Maki, M.6
  • 53
    • 0028148057 scopus 로고
    • Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with calmodulin-like domain of the proteinase
    • Ma, H., H. Q. Yang, E. Takano, M. Hatanaka, and M. Maki. 1994. Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with calmodulin-like domain of the proteinase. J. Biol. Chem. 269:24430-24436.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24430-24436
    • Ma, H.1    Yang, H.Q.2    Takano, E.3    Hatanaka, M.4    Maki, M.5
  • 55
    • 0027615958 scopus 로고
    • Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers
    • Morgan, J. B., T. L. Wheeler, M. Koohmaraie, J. W. Savell, and J. D. Crouse. 1993. Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers. J. Anim. Sci. 71:1471-1476.
    • (1993) J. Anim. Sci. , vol.71 , pp. 1471-1476
    • Morgan, J.B.1    Wheeler, T.L.2    Koohmaraie, M.3    Savell, J.W.4    Crouse, J.D.5
  • 56
    • 84985294862 scopus 로고
    • CAF activity, calcium concentration, and the 30,000-dalton component of tough and tender bovine longissimus muscle
    • Parrish, F. C., Jr., C. J. Selvig, R. D. Culler, and M. G. Zeece. 1981. CAF activity, calcium concentration, and the 30,000-dalton component of tough and tender bovine longissimus muscle. J. Food Sci. 46:308-309+.
    • (1981) J. Food Sci. , vol.46
    • Parrish F.C., Jr.1    Selvig, C.J.2    Culler, R.D.3    Zeece, M.G.4
  • 57
    • 84985204367 scopus 로고
    • Effect of postmortem storage on titin and nebulin in pork and poultry light and dark muscle
    • Paxhia, J. M., and F. C. Parrish, Jr. 1988. Effect of postmortem storage on titin and nebulin in pork and poultry light and dark muscle. J. Food Sci. 53:1599-1601+.
    • (1988) J. Food Sci. , vol.53
    • Paxhia, J.M.1    Parrish F.C., Jr.2
  • 58
    • 0014321738 scopus 로고
    • Determination of proteins in "Tris" buffer by the biuret reaction
    • Robson, R. M., D. E. Goll, and M. J. Temple. 1968. Determination of proteins in "Tris" buffer by the biuret reaction. Anal. Biochem. 24:339-341.
    • (1968) Anal. Biochem. , vol.24 , pp. 339-341
    • Robson, R.M.1    Goll, D.E.2    Temple, M.J.3
  • 59
    • 0026454458 scopus 로고
    • Positive regulation of μ-calpain action by polyphosphoinositides
    • Saido, T. C., M. Shibata, T. Takenawa, H. Murofushi, and K. Suzuki. 1992. Positive regulation of μ-calpain action by polyphosphoinositides. J. Biol. Chem. 267:24585-24590.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24585-24590
    • Saido, T.C.1    Shibata, M.2    Takenawa, T.3    Murofushi, H.4    Suzuki, K.5
  • 60
    • 0021779754 scopus 로고
    • 2+-dependent proteinase
    • E. A. Khairallah, J.W.C. Bird, and J. S. Bond (Ed.) Alan R. Liss, New York
    • 2+-dependent proteinase. In: E. A. Khairallah, J.W.C. Bird, and J. S. Bond (Ed.) Intracellular Protein Catabolism. pp 257-259. Alan R. Liss, New York.
    • (1985) Intracellular Protein Catabolism. , pp. 257-259
    • Shannon, J.D.1    Goll, D.E.2
  • 61
    • 0038739604 scopus 로고
    • Calcium-dependent proteinase: A novel molecular species, regulation of gene expression, and activation at the cell membrane
    • A. Guidoffi (Ed.) Raven Press, New York
    • Suzuki, K., H. Sorimachi, A. Hata, S. Ohno, Y. Emori, H. Kawasaki, T. Saido, S. Imajoh-Ohmi, and Y. Akita. 1990. Calcium-dependent proteinase: a novel molecular species, regulation of gene expression, and activation at the cell membrane. In: A. Guidoffi (Ed.) Neurotoxicity of Excitatory Amino Acids, pp 79-93. Raven Press, New York.
    • (1990) Neurotoxicity of Excitatory Amino Acids , pp. 79-93
    • Suzuki, K.1    Sorimachi, H.2    Hata, A.3    Ohno, S.4    Emori, Y.5    Kawasaki, H.6    Saido, T.7    Imajoh-Ohmi, S.8    Akita, Y.9
  • 63
    • 0002932128 scopus 로고
    • Enzyme localization during postmortem muscle tenderization
    • A. Ouali, D. I. DeMeyer, and F.J.M. Smulders (Ed.) EC\CE/AMST, Utrecht, The Netherlands
    • Taylor, R. G., D. E. Goll, and A. Ouali. 1995b. Enzyme localization during postmortem muscle tenderization. In: A. Ouali, D. I. DeMeyer, and F.J.M. Smulders (Ed.) Expression of Tissue Proteinases and Regulation of Protein Degradation. pp 347-358. EC\CE/AMST, Utrecht, The Netherlands.
    • (1995) Expression of Tissue Proteinases and Regulation of Protein Degradation , pp. 347-358
    • Taylor, R.G.1    Goll, D.E.2    Ouali, A.3
  • 64
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 65
    • 0021738226 scopus 로고
    • Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes
    • Twining, S. S. 1984. Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal. Biochem. 143:30-34.
    • (1984) Anal. Biochem. , vol.143 , pp. 30-34
    • Twining, S.S.1
  • 66
    • 0020851698 scopus 로고
    • 2+-dependent neutral proteinases and their specific inhibitor during post-mortem storage of rabbit muscle
    • 2+-dependent neutral proteinases and their specific inhibitor during post-mortem storage of rabbit muscle. J. Sci. Food Agric. 34:1241-1250.
    • (1983) J. Sci. Food Agric. , vol.34 , pp. 1241-1250
    • Vidalenc, P.1    Cottin, P.2    Merdaci, N.3    Ducastaing, A.4
  • 67
    • 0026145068 scopus 로고
    • A modified procedure for simultaneous extraction and subsequent assay of calcium-dependent and lysosomal protease systems from a skeletal muscle biopsy
    • Wheeler, T. L., and M. Koohmaraie. 1991. A modified procedure for simultaneous extraction and subsequent assay of calcium-dependent and lysosomal protease systems from a skeletal muscle biopsy. J. Anim. Sci. 69:1559-1565.
    • (1991) J. Anim. Sci. , vol.69 , pp. 1559-1565
    • Wheeler, T.L.1    Koohmaraie, M.2
  • 68
    • 0028432852 scopus 로고
    • Prerigor and postrigor changes in tenderness of ovine longissimus muscle
    • Wheeler, T. L., and M. Koohmaraie. 1994. Prerigor and postrigor changes in tenderness of ovine longissimus muscle. J. Anim. Sci. 72:1232-1238.
    • (1994) J. Anim. Sci. , vol.72 , pp. 1232-1238
    • Wheeler, T.L.1    Koohmaraie, M.2
  • 69
    • 0026248168 scopus 로고
    • Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride
    • Whipple, G., and M. Koohmaraie. 1991. Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride. J. Anim. Sci. 69:4449-4460.
    • (1991) J. Anim. Sci. , vol.69 , pp. 4449-4460
    • Whipple, G.1    Koohmaraie, M.2
  • 70
    • 0026825122 scopus 로고
    • Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on post-mortem proteolysis
    • Whipple, G., and M. Koohmaraie. 1992. Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on post-mortem proteolysis. J. Anim. Sci. 70:798-804.
    • (1992) J. Anim. Sci. , vol.70 , pp. 798-804
    • Whipple, G.1    Koohmaraie, M.2
  • 71
    • 0025518205 scopus 로고
    • Effects of high-temperature conditioning on enzymatic activity and tenderness of Bos indicus longissimus muscle
    • Whipple, G., M. Koohmaraie, M. E. Dikeman, and J. D. Crouse. 1990. Effects of high-temperature conditioning on enzymatic activity and tenderness of Bos indicus longissimus muscle. J. Anim. Sci. 68:3654-3662.
    • (1990) J. Anim. Sci. , vol.68 , pp. 3654-3662
    • Whipple, G.1    Koohmaraie, M.2    Dikeman, M.E.3    Crouse, J.D.4
  • 73
    • 0001437090 scopus 로고
    • Effect of calcium activated protease (CAF) on bovine myofibrils under different conditions of pH and temperature
    • Zeece, M. G., R. M. Robson, M. L. Lusby, and F. C. Parrish, Jr. 1986. Effect of calcium activated protease (CAF) on bovine myofibrils under different conditions of pH and temperature. J. Food Sci. 51:797-803.
    • (1986) J. Food Sci. , vol.51 , pp. 797-803
    • Zeece, M.G.1    Robson, R.M.2    Lusby, M.L.3    Parrish F.C., Jr.4
  • 74
    • 0025911090 scopus 로고
    • Two-stage autolysis of the catalytic subunit initiates activation of calpain I
    • Zimmerman, U.-J., and W. W. Schlaepfer. 1991. Two-stage autolysis of the catalytic subunit initiates activation of calpain I. Biochim. Biophys. Acta 1078:192-198.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 192-198
    • Zimmerman, U.-J.1    Schlaepfer, W.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.