메뉴 건너뛰기




Volumn 118, Issue 3, 1997, Pages 523-529

Purification and characterization of cathepsin L-like enzyme from the muscle of anchovy, Engraulis japonica

Author keywords

Anchovy; Anchovy sauce; Cathepsin L; Engraulis japonica; Enzyme purification; Fish fermentation; Kinetics

Indexed keywords

CATHEPSIN L; PROTEINASE;

EID: 0031418662     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(97)00181-8     Document Type: Article
Times cited : (29)

References (31)
  • 1
    • 84919617127 scopus 로고
    • Cathepsin degradation of Pacific whiting surimi proteins
    • An, H.; Weerasinghe, V.; Seymour, T.A.; Morrissey, M.T. Cathepsin degradation of Pacific whiting surimi proteins. J. Food Sci. 59:1013-1017, 1033;1994.
    • (1994) J. Food Sci. , vol.59 , pp. 1013-1017
    • An, H.1    Weerasinghe, V.2    Seymour, T.A.3    Morrissey, M.T.4
  • 2
    • 0002559619 scopus 로고
    • Isolation and activation of cathepsin L-inhibitor complex from Pacific whiting (Merluccius productus)
    • An, H.; Peters, M.Y.; Seymour, T.A.; Morrissey, M.T. Isolation and activation of cathepsin L-inhibitor complex from Pacific whiting (Merluccius productus). J. Agric. Food Chem. 43: 327-330;1995.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 327-330
    • An, H.1    Peters, M.Y.2    Seymour, T.A.3    Morrissey, M.T.4
  • 3
    • 0023461195 scopus 로고
    • Endogenous proteolytic enzymes in skeletal muscle: Their significance in muscle physiology and during postmortem aging events in carcasses
    • Asghar, A.; Bhatti, A.R. Endogenous proteolytic enzymes in skeletal muscle: their significance in muscle physiology and during postmortem aging events in carcasses. Adv. Food Res. 31:343-451;1977.
    • (1977) Adv. Food Res. , vol.31 , pp. 343-451
    • Asghar, A.1    Bhatti, A.R.2
  • 4
    • 0015338074 scopus 로고
    • A new assay for cathepsin Bl and other thiol proteinases
    • Barrett, A.J. A new assay for cathepsin Bl and other thiol proteinases. Anal. Biochem. 47:280-293;1972.
    • (1972) Anal. Biochem. , vol.47 , pp. 280-293
    • Barrett, A.J.1
  • 5
    • 0017142632 scopus 로고
    • An improved color reagent for use in Barrett's assay of cathepsin B
    • Barrett, A.J. An improved color reagent for use in Barrett's assay of cathepsin B. Anal. Biochem. 76:374-376;1976.
    • (1976) Anal. Biochem. , vol.76 , pp. 374-376
    • Barrett, A.J.1
  • 7
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H and cathepsin L
    • Barret, A.J.; Kirschke, H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 80:535-561;1981.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barret, A.J.1    Kirschke, H.2
  • 8
    • 0017592831 scopus 로고
    • Degradation of myofibrillar proteins by cathepsin B and D
    • Bird, J.W.C.; Schwartz, W.N.; Spanier, A.M. Degradation of myofibrillar proteins by cathepsin B and D. Acta Biol. Med. Germ. 36:1587-1604;1977.
    • (1977) Acta Biol. Med. Germ. , vol.36 , pp. 1587-1604
    • Bird, J.W.C.1    Schwartz, W.N.2    Spanier, A.M.3
  • 9
    • 84861748813 scopus 로고
    • Partial purification and characterization of cathepsin D-like and B-like acid protease from surf clam viscera
    • Chen, H.C.; Zall, R.R. Partial purification and characterization of cathepsin D-like and B-like acid protease from surf clam viscera. J. Food Sci. 51:1-75, 78;1986.
    • (1986) J. Food Sci. , vol.51 , pp. 1-75
    • Chen, H.C.1    Zall, R.R.2
  • 10
    • 78651153791 scopus 로고
    • Disc-electrophoresis-II, method and application to human serum protein
    • Davis, B.J. Disc-electrophoresis-II, method and application to human serum protein. Ann. N. Y. Acad. Sci. 121:404-427; 1964.
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 11
    • 0028802456 scopus 로고
    • Comparison of trypsin and chymotrypsin from the viscera of anchovy, Engraulis japonica
    • Heu, M.S.; Kim, H.R.; Pyeun, J.H. Comparison of trypsin and chymotrypsin from the viscera of anchovy, Engraulis japonica. Comp. Biochem. Physiol. 112B:557-567;1995.
    • (1995) Comp. Biochem. Physiol. , vol.112 B , pp. 557-567
    • Heu, M.S.1    Kim, H.R.2    Pyeun, J.H.3
  • 12
    • 0015500932 scopus 로고
    • Determination of tryptophan content of protein by ion exchange chromatograph of alkaline hydrolysates
    • Hugli, T.E.; Moore, S.J. Determination of tryptophan content of protein by ion exchange chromatograph of alkaline hydrolysates. J. Biol. Chem. 247:2828-2834;1972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2828-2834
    • Hugli, T.E.1    Moore, S.J.2
  • 13
    • 0015459835 scopus 로고
    • Effect of antipain on lysosomal peptide-hydrolyases from swine liver
    • Ikezawa, H.; Yamada, K.; Aoyagi, T.; Takeuchi, T.; Umezawa, H. Effect of antipain on lysosomal peptide-hydrolyases from swine liver. J. Antibiot. 25:738-746;1972.
    • (1972) J. Antibiot. , vol.25 , pp. 738-746
    • Ikezawa, H.1    Yamada, K.2    Aoyagi, T.3    Takeuchi, T.4    Umezawa, H.5
  • 14
    • 3743051463 scopus 로고
    • The proteinase distributed in the intestinal organs of fish. 2. Characterization of the three alkaline proteinases from the pyloric caeca of mackerel Scomber japonicus
    • Kim, H.R.; Pyeun, J.H. The proteinase distributed in the intestinal organs of fish. 2. Characterization of the three alkaline proteinases from the pyloric caeca of mackerel Scomber japonicus. Bull. Korean Fish. Soc. 19:547-557;1986.
    • (1986) Bull. Korean Fish. Soc. , vol.19 , pp. 547-557
    • Kim, H.R.1    Pyeun, J.H.2
  • 16
    • 0025607120 scopus 로고
    • Comparative study on specificities of rat cathepsin L and papain: Amino acid differences at substrate-binding sites are involved in their specificities
    • Koga, H.; Yamada, H.; Nishimura, Y.; Kato, K.; Imoto, T. Comparative study on specificities of rat cathepsin L and papain: Amino acid differences at substrate-binding sites are involved in their specificities. J. Biochem. 108:976-982;1990.
    • (1990) J. Biochem. , vol.108 , pp. 976-982
    • Koga, H.1    Yamada, H.2    Nishimura, Y.3    Kato, K.4    Imoto, T.5
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of Bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227:680-686; 1970.
    • (1970) Nature , vol.227 , pp. 680-686
    • Laemmli, U.K.1
  • 18
    • 77957773738 scopus 로고
    • Purification and characterization of proteinases identified as cathepsin L and L-like (58 KDa) proteinase from mackerel (Scomber australasicus)
    • Lee, J.J.; Chen, H.C.; Jiang, S.T. Purification and characterization of proteinases identified as cathepsin L and L-like (58 KDa) proteinase from mackerel (Scomber australasicus). Biosci. Biotechnol. Biochem. 57:1470-1476;1993.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1470-1476
    • Lee, J.J.1    Chen, H.C.2    Jiang, S.T.3
  • 20
    • 85008137455 scopus 로고
    • Isolation and characterization of the protease responsible for jellification of Pacific hake muscle
    • Masaki, T.; Shimomukai, M.; Miyauchi, Y.; Ono, S.; Tuchiya, T.; Matsuda, T. Isolation and characterization of the protease responsible for jellification of Pacific hake muscle. Nippon Suisan Gakkaishi 59:683-690;1993.
    • (1993) Nippon Suisan Gakkaishi , vol.59 , pp. 683-690
    • Masaki, T.1    Shimomukai, M.2    Miyauchi, Y.3    Ono, S.4    Tuchiya, T.5    Matsuda, T.6
  • 21
    • 0021313131 scopus 로고
    • The purification and properties of cathepsin L from rabbit liver
    • Mason, R.W.; Taylor, M.A.; Etherington, D.J. The purification and properties of cathepsin L from rabbit liver. Biochem. J. 217:209-217;1984.
    • (1984) Biochem. J. , vol.217 , pp. 209-217
    • Mason, R.W.1    Taylor, M.A.2    Etherington, D.J.3
  • 22
    • 84893743812 scopus 로고
    • Effect of protease inhibitors on torsion measurements and autolysis of Pacific whiting surimi
    • Morrissey, M.T.; Wu, J.W.; Lin, D.; An, H. Effect of protease inhibitors on torsion measurements and autolysis of Pacific whiting surimi. J. Food Sci. 58:1050-1054;1993.
    • (1993) J. Food Sci. , vol.58 , pp. 1050-1054
    • Morrissey, M.T.1    Wu, J.W.2    Lin, D.3    An, H.4
  • 23
    • 0018940824 scopus 로고
    • Purification and some properties of a myofibrillar protein-degrading protease, cathepsin L from rabbit skeletal muscle
    • Okitani, A.; Matsukyra, U.; Kato, H.; Juhimaki, M. Purification and some properties of a myofibrillar protein-degrading protease, cathepsin L from rabbit skeletal muscle. J. Biochem. 87:1133-1143;1980.
    • (1980) J. Biochem. , vol.87 , pp. 1133-1143
    • Okitani, A.1    Matsukyra, U.2    Kato, H.3    Juhimaki, M.4
  • 24
    • 0344788840 scopus 로고
    • The proteinase distributed in the intestinal organs offish. 1. Purification of the three alkaline proteinases from the pyloric caeca of mackerel, Scomber japonicus
    • Pyeun, J.H.; Kim, H.R. The proteinase distributed in the intestinal organs offish. 1. Purification of the three alkaline proteinases from the pyloric caeca of mackerel, Scomber japonicus. Bull. Korean Fish. Soc. 19:537-546;1986.
    • (1986) Bull. Korean Fish. Soc. , vol.19 , pp. 537-546
    • Pyeun, J.H.1    Kim, H.R.2
  • 25
    • 0347389084 scopus 로고
    • The proteinase distributed in the intestinal organs of fish. 3. Purification and some enzymatic properties of the alkaline proteinases from the pyloric caeca of skipjack, Katsuwonus vagans
    • Pyeun, J.H.; Kim, H.R.; Heu, M.S. The proteinase distributed in the intestinal organs of fish. 3. Purification and some enzymatic properties of the alkaline proteinases from the pyloric caeca of skipjack, Katsuwonus vagans. Bull. Korean Fish. Soc. 21:85-96;1988.
    • (1988) Bull. Korean Fish. Soc. , vol.21 , pp. 85-96
    • Pyeun, J.H.1    Kim, H.R.2    Heu, M.S.3
  • 26
  • 27
    • 0014679375 scopus 로고
    • A new convenient method for estimation of total cystine-cysteine in proteins
    • Spencer, R.L.; Wold, F. A new convenient method for estimation of total cystine-cysteine in proteins. Anal. Biochem. 32: 185-190;1969.
    • (1969) Anal. Biochem. , vol.32 , pp. 185-190
    • Spencer, R.L.1    Wold, F.2
  • 28
    • 84952513849 scopus 로고
    • Characterization of a heat stable protease from arrowtooth flunder, Atheresthes stomias
    • Wasson, D.H.; Babbitt, J.K.; French, J.S. Characterization of a heat stable protease from arrowtooth flunder, Atheresthes stomias. J. Aquat. Food Prod. Technol. 1:167-182;1992.
    • (1992) J. Aquat. Food Prod. Technol. , vol.1 , pp. 167-182
    • Wasson, D.H.1    Babbitt, J.K.2    French, J.S.3
  • 29
    • 0025368356 scopus 로고
    • Purification and characterization of cathepsin L from the white muscle of chum salmon (Oncorhynchus keta)
    • Yamashita, M.; Konagaya, S. 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
  • 30
    • 85008070248 scopus 로고
    • Participation of cathepsin L in extensive softening of the muscle of chum salmon caught during spawning migration
    • Yamashita, M.; Konagaya, S. Participation of cathepsin L in 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
  • 31
    • 0026489465 scopus 로고
    • An enzyme-inhibitor complex of cathepsin L in the white muscle of chum salmon (Oncorhynchus keta) in spawning migration
    • Yamashita, M.; Konagaya, S. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.