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Volumn 82, Issue 5, 2004, Pages 1475-1481

Bovine metalloprotease characterization and in vitro connective tissue degradation

Author keywords

Bovine; Collagen; Collagenase; Enzyme; Meat Tenderness; Metalloprotease

Indexed keywords

BOVINAE;

EID: 2442465934     PISSN: 00218812     EISSN: None     Source Type: Journal    
DOI: 10.2527/2004.8251475x     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 84985330464 scopus 로고
    • The basis of meat texture
    • Bailey, A. J. 1972. The basis of meat texture. J. Sci. Food Agric. 23:995-1007.
    • (1972) J. Sci. Food Agric. , vol.23 , pp. 995-1007
    • Bailey, A.J.1
  • 3
    • 0023777072 scopus 로고
    • Bacterial collagenase and collagen identification
    • Berry, L., and C. A. Shuttleworth. 1988. Bacterial collagenase and collagen identification. Connect. Tissue Res. 17:217-222.
    • (1988) Connect. Tissue Res. , vol.17 , pp. 217-222
    • Berry, L.1    Shuttleworth, C.A.2
  • 6
    • 0021325829 scopus 로고
    • Extracts of human articular cartilage contain an inhibitor of tissue metalloproteases
    • Dean, D. D., and J. F. Woessner. 1984. Extracts of human articular cartilage contain an inhibitor of tissue metalloproteases. Biochem. J. 218:277-283.
    • (1984) Biochem. J. , vol.218 , pp. 277-283
    • Dean, D.D.1    Woessner, J.F.2
  • 7
    • 0000051107 scopus 로고
    • Tenderization of beef with bacterial collagenase
    • Foegeding, E. A., and D. K. Larick. 1986. Tenderization of beef with bacterial collagenase. Meat Sci. 18:201-210.
    • (1986) Meat Sci. , vol.18 , pp. 201-210
    • Foegeding, E.A.1    Larick, D.K.2
  • 8
    • 0026654155 scopus 로고
    • Staining for enzymatic activity after gel electrophoresis, I
    • Gabriel, O., and D. M. Gersten. 1992. Staining for enzymatic activity after gel electrophoresis, I. Anal. Biochem. 203:1-21.
    • (1992) Anal. Biochem. , vol.203 , pp. 1-21
    • Gabriel, O.1    Gersten, D.M.2
  • 9
    • 0020549450 scopus 로고
    • Purification and characterization of a rabbit bone metalloproteinase that degrades proteoglycan and other connective tissue components
    • Galloway, W. A., G. Murphy, J. D. Sandy, J. Gavrilovic, T. E. Cawston, and J. J. Reynolds. 1983. Purification and characterization of a rabbit bone metalloproteinase that degrades proteoglycan and other connective tissue components. Biochem. J. 209:741-752.
    • (1983) Biochem. J. , vol.209 , pp. 741-752
    • Galloway, W.A.1    Murphy, G.2    Sandy, J.D.3    Gavrilovic, J.4    Cawston, T.E.5    Reynolds, J.J.6
  • 10
    • 0025255109 scopus 로고
    • One-dimensional gel electrophoresis
    • Garfin, D. E. 1990. One-dimensional gel electrophoresis. Methods Enzymol. 182:425-441.
    • (1990) Methods Enzymol. , vol.182 , pp. 425-441
    • Garfin, D.E.1
  • 12
    • 0015856003 scopus 로고
    • The isolation of collagenase and its enzymological and physico-chemical properties
    • Hanada, K., T. Mizutani, M. Yamagishi, H. Suji, T. Misaki, and J. Sawada. 1973. The isolation of collagenase and its enzymological and physico-chemical properties. Agric. Biol. Chem. 37:1771-1781.
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 1771-1781
    • Hanada, K.1    Mizutani, T.2    Yamagishi, M.3    Suji, H.4    Misaki, T.5    Sawada, J.6
  • 13
    • 0016383464 scopus 로고
    • Influence of temperature and fibril stability on degradation of cartilage collagen by rheumatoid synovial collagenase
    • Harris, E. D., and P. A. McCroskery. 1974. Influence of temperature and fibril stability on degradation of cartilage collagen by rheumatoid synovial collagenase. New Engl. J. Med. 290:1-6.
    • (1974) New Engl. J. Med. , vol.290 , pp. 1-6
    • Harris, E.D.1    McCroskery, P.A.2
  • 14
  • 15
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen, C., and E. B. Dowdle. 1980. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem. 102:196-202.
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 16
    • 84986466174 scopus 로고
    • Degradation of various meat fractions by tenderizing enzymes
    • Kang, C. K., and E. E. Rice. 1970. Degradation of various meat fractions by tenderizing enzymes. J. Food Sci. 35:563-577.
    • (1970) J. Food Sci. , vol.35 , pp. 563-577
    • Kang, C.K.1    Rice, E.E.2
  • 17
    • 0002514983 scopus 로고
    • Muscle proteinases and meat ageing
    • Koohmaraie, M. 1994. Muscle proteinases and meat ageing. Meat Sci. 16:93-104.
    • (1994) Meat Sci. , vol.16 , pp. 93-104
    • Koohmaraie, M.1
  • 18
    • 84985208668 scopus 로고
    • ++-dependent proteases and lysosomal enzymes in postmortem changes in bovine skeletal muscle
    • ++-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
  • 19
    • 0019139168 scopus 로고
    • Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate
    • Lacks, S. A., and S. S. Springhorn. 1980. Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. J. Biol. Chem. 255:7467-7473.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7467-7473
    • Lacks, S.A.1    Springhorn, S.S.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0348088612 scopus 로고
    • The flexibility of the collagen compartment of muscle
    • McCormick, R. J. 1994. The flexibility of the collagen compartment of muscle. Meat Sci. 36:79-91.
    • (1994) Meat Sci. , vol.36 , pp. 79-91
    • McCormick, R.J.1
  • 23
    • 0017735281 scopus 로고
    • The detection and characterization of collagenase inhibitors from rabbit tissue cultures
    • Murphy, G., T. E. Cawston, and J. J. Reynolds. 1981. The detection and characterization of collagenase inhibitors from rabbit tissue cultures. Biochim. Biophys. Acta 483:493-502.
    • (1981) Biochim. Biophys. Acta , vol.483 , pp. 493-502
    • Murphy, G.1    Cawston, T.E.2    Reynolds, J.J.3
  • 24
    • 0031992372 scopus 로고    scopus 로고
    • Changes in mechanical strength of intramuscular connective tissue during postmortem aging of beef
    • Nishimura, T., A. Liu, A. Hattori, and K. Takahashi. 1998. Changes in mechanical strength of intramuscular connective tissue during postmortem aging of beef. J. Anim. Sci. 76:528-532.
    • (1998) J. Anim. Sci. , vol.76 , pp. 528-532
    • Nishimura, T.1    Liu, A.2    Hattori, A.3    Takahashi, K.4
  • 25
    • 0023024460 scopus 로고
    • A Metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components
    • Okada, Y., H. Nagase, and E. D. Harris. 1986. A Metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. J. Biol. Chem. 261:14245-14255.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14245-14255
    • Okada, Y.1    Nagase, H.2    Harris, E.D.3
  • 26
    • 0000337085 scopus 로고
    • The enzymology of conditioning
    • R. A. Lawrie, ed. Applied Science Publishers, Ltd., London
    • Penny, I. F. 1980. The enzymology of conditioning. Page 115 in Developments in Meat Science - 1. R. A. Lawrie, ed. Applied Science Publishers, Ltd., London.
    • (1980) Developments in Meat Science , vol.1 , pp. 115
    • Penny, I.F.1
  • 27
  • 30
    • 0000215063 scopus 로고
    • The effects of conditioning on meat collagen: Part 1 - Evidence for gross in situ proteolysis
    • Stanton, C., and N. Light. 1987. The effects of conditioning on meat collagen: Part 1 - Evidence for gross in situ proteolysis. Meat Sci. 21:249-265.
    • (1987) Meat Sci. , vol.21 , pp. 249-265
    • Stanton, C.1    Light, N.2
  • 31
    • 84989662497 scopus 로고
    • Biochemistry and physiology of mammalian collagenases
    • M. E. Nimni, ed. CRC Press, Boca Raton, FL
    • Stricklin, G. P., and M. S. Hibbs. 1988. Biochemistry and physiology of mammalian collagenases. Page 187 in Collagen: Volume I, Biochemistry. M. E. Nimni, ed. CRC Press, Boca Raton, FL.
    • (1988) Collagen: Volume I, Biochemistry , vol.1 , pp. 187
    • Stricklin, G.P.1    Hibbs, M.S.2
  • 32
    • 0030305246 scopus 로고    scopus 로고
    • Structural weakening of skeletal muscle tissue during post-mortem ageing of meat: The non-enzymatic mechanism of meat tenderization
    • Takahashi, K. 1996. Structural weakening of skeletal muscle tissue during post-mortem ageing of meat: The non-enzymatic mechanism of meat tenderization. Meat Sci. 43:S67-S80.
    • (1996) Meat Sci. , vol.43
    • Takahashi, K.1
  • 33
    • 0019857661 scopus 로고
    • The collagen substrate specificity of human skin fibroblast collagenase
    • Welgus, H. G., J. J. Jeffrey, and A. Z. Eisen. 1981. The collagen substrate specificity of human skin fibroblast collagenase. J. Biol. Chem. 256:9511-9515.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9511-9515
    • Welgus, H.G.1    Jeffrey, J.J.2    Eisen, A.Z.3
  • 34
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner, J. F. 1991. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5:2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner, J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.