메뉴 건너뛰기




Volumn 63, Issue 5, 1997, Pages 824-829

Purification and Some Properties of a Latent Form Cathepsin L from Mackerel White Muscle

Author keywords

Cathepsin L; Cysteine protease; Mackerel muscle; Purification

Indexed keywords

SCOMBER JAPONICUS;

EID: 0000988814     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.2331/fishsci.63.824     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 85008070248 scopus 로고
    • Participation of cathepsin L into extensive softening of the muscle of chum salmon caught during spawning migration
    • M. Yamashita and S. Konagaya: Participation of cathepsin L into extensive softening of the muscle of chum salmon caught during spawning migration. Nippon Suisan Gakkaishi, 56, 1271-1277 (1990).
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 1271-1277
    • Yamashita, M.1    Konagaya, S.2
  • 2
    • 0026458505 scopus 로고
    • Differentiation and localization of catheptic proteinases responsible for extensive autolysis of mature chum salmon muscle (Oncorhynchus keta)
    • M. Yamashita and S. Konagaya: Differentiation and localization of catheptic proteinases responsible for extensive autolysis of mature chum salmon muscle (Oncorhynchus keta). Comp. Biochem. Physiol., 103B, 999-1003 (1992).
    • (1992) Comp. Biochem. Physiol. , vol.103 B , pp. 999-1003
    • Yamashita, M.1    Konagaya, S.2
  • 4
    • 0025186654 scopus 로고
    • High activities of cathepsins B, D, H and L in the white muscle of chum salmon in spawning migration
    • M. Yamashita and S. Konagaya: High activities of cathepsins B, D, H and L in the white muscle of chum salmon in spawning migration. Comp. Biochem. Physiol., 95B, 149-152 (1990).
    • (1990) Comp. Biochem. Physiol. , vol.95 B , pp. 149-152
    • Yamashita, M.1    Konagaya, S.2
  • 5
    • 0025368356 scopus 로고
    • Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta
    • M. Yamashita and S. Konagaya: Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta. Comp. Biochem. Physiol., 96B, 247-252 (1990).
    • (1990) Comp. Biochem. Physiol. , vol.96 B , pp. 247-252
    • Yamashita, M.1    Konagaya, S.2
  • 6
    • 0023462882 scopus 로고
    • The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L
    • R. W. Mason, S. Gal, and M. M. Gottesman: The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L. Biochem. J., 248, 449-454 (1987).
    • (1987) Biochem. J. , vol.248 , pp. 449-454
    • Mason, R.W.1    Gal, S.2    Gottesman, M.M.3
  • 7
    • 0024491503 scopus 로고
    • The identification of active forms of cysteine proteinases in Kirsten-virus-transformed mous fibroblasts by use of a specific radiolabelled inhibitor
    • R. W. Mason, D. Wilcox, P. Wikstrom, and E. N. Shaw: The identification of active forms of cysteine proteinases in Kirsten-virus-transformed mous fibroblasts by use of a specific radiolabelled inhibitor. Biochem. J., 257, 125-129 (1989).
    • (1989) Biochem. J. , vol.257 , pp. 125-129
    • Mason, R.W.1    Wilcox, D.2    Wikstrom, P.3    Shaw, E.N.4
  • 9
    • 0028237920 scopus 로고
    • Maturation of human procathepsin B
    • L. Mach, J. S. Mort, and J. Glössl: Maturation of human procathepsin B. J. Biol. Chem., 269, 13030-13035 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 13030-13035
    • Mach, L.1    Mort, J.S.2    Glössl, J.3
  • 10
    • 0023905240 scopus 로고
    • Identification of latent procathepsins B and L in microsomal lumen. Characterization of enzymatic activation and proteolytic processing in vitro
    • Y. Nishimura, T. Kawabata, and K. Kato: Identification of latent procathepsins B and L in microsomal lumen. Characterization of enzymatic activation and proteolytic processing in vitro. Arch. Biochem. Biophys., 261, 64-71 (1988).
    • (1988) Arch. Biochem. Biophys. , vol.261 , pp. 64-71
    • Nishimura, Y.1    Kawabata, T.2    Kato, K.3
  • 11
    • 0024339693 scopus 로고
    • The processing of a cathepsin L precursor in vitro
    • B. Wiederanders and H. Kirschke: The processing of a cathepsin L precursor in vitro. Arch. Biochem. Biophys., 272, 516-521 (1989).
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 516-521
    • Wiederanders, B.1    Kirschke, H.2
  • 12
    • 0024284203 scopus 로고
    • Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages
    • K. Hara, E. Kominami, and N. Katunuma: Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages. FEBS Lett., 231, 229-231 (1988).
    • (1988) FEBS Lett. , vol.231 , pp. 229-231
    • Hara, K.1    Kominami, E.2    Katunuma, N.3
  • 16
  • 17
    • 0026489465 scopus 로고
    • An enzyme-inhibitor complex of cathepsin L in the white muscle of chum salmon (Oncorhynchus keta) in spawning migration
    • M. Yamashita and S. Konagaya: An enzyme-inhibitor complex of cathepsin L in the white muscle of chum salmon (Oncorhynchus keta) in spawning migration. Comp. Biochem. Physiol., 103B, 1005-1010 (1992).
    • (1992) Comp. Biochem. Physiol. , vol.103 B , pp. 1005-1010
    • Yamashita, M.1    Konagaya, S.2
  • 18
    • 84986532390 scopus 로고
    • Purification and properties of carp muscle cathepsin D
    • Y. Makinodan, T. Akasaka, H. Toyohara, and S. Ikeda: Purification and properties of carp muscle cathepsin D. J. Food Sci., 47, 647-652 (1982).
    • (1982) J. Food Sci. , vol.47 , pp. 647-652
    • Makinodan, Y.1    Akasaka, T.2    Toyohara, H.3    Ikeda, S.4
  • 19
    • 85011183760 scopus 로고
    • Purification and characterization of a cathepsin B-like enzyme from mackerel white muscle
    • T. Aoki, T. Yamashita, and R. Ueno: Purification and characterization of a cathepsin B-like enzyme from mackerel white muscle. Fisheries Sci., 61, 121-126 (1995).
    • (1995) Fisheries Sci. , vol.61 , pp. 121-126
    • Aoki, T.1    Yamashita, T.2    Ueno, R.3
  • 22
    • 78651153791 scopus 로고
    • Disc electrophoresis-II. Method and application to human serum proteins
    • B. J. Davis: Disc electrophoresis-II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci., 121, 404-427 (1964).
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 23
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • K. Weber and M. Osborn: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem., 244, 4406-4412 (1969).
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 24
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • ed. by L. Lorand, Academic Press, New York
    • A. J. Barrett and H. Kirschke: Cathepsin B, cathepsin H, and cathepsin L, in "Methods in Enzymology" (ed. by L. Lorand), Academic Press, New York, 1981, pp. 535-561.
    • (1981) Methods in Enzymology , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 26
    • 0023778543 scopus 로고
    • Isolation and sequence of a cDNa for human pro-(cathepsin L)
    • S. Gal and M. M. Gottesman: Isolation and sequence of a cDNA for human pro-(cathepsin L). Biochem. J., 253, 303-306 (1988).
    • (1988) Biochem. J. , vol.253 , pp. 303-306
    • Gal, S.1    Gottesman, M.M.2
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. M. Bradford: 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).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.