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Volumn 6, Issue 3, 1998, Pages 129-135

Purification and characterization of a novel dipeptidase from carp ordinary muscle

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; ENZYME; FISH;

EID: 0031735045     PISSN: 09412905     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (38)
  • 2
    • 84919617127 scopus 로고
    • Cathepsin degradation of Pacific whiting surimi proteins
    • An H, Weerasinghe V, Seymour TA, Morrissey MT (1994) Cathepsin degradation of Pacific whiting surimi proteins. J Food Sci 59:1013-1017
    • (1994) J Food Sci , vol.59 , pp. 1013-1017
    • An, H.1    Weerasinghe, V.2    Seymour, T.A.3    Morrissey, M.T.4
  • 3
    • 0023461195 scopus 로고
    • Endogenous proteolytic enzymes in skeletal muscle: Their significance in physiology and during postmortem aging events in carcasses
    • Asghar A, Bhatti AR (1987) Endogenous proteolytic enzymes in skeletal muscle: Their significance in physiology and during postmortem aging events in carcasses. Adv Food Res 31:343-451
    • (1987) Adv Food Res , vol.31 , pp. 343-451
    • Asghar, A.1    Bhatti, A.R.2
  • 4
    • 0008422651 scopus 로고
    • Fish muscle as food
    • Bechtel PJ (ed). Academic Press, London
    • Brown WD (1986) Fish muscle as food. In: Bechtel PJ (ed). Muscle as food. Academic Press, London, pp 406-451
    • (1986) Muscle as Food , pp. 406-451
    • Brown, W.D.1
  • 5
    • 0014006562 scopus 로고
    • The purification and properties of a particulate renal dipeptidase
    • Campbell BJ, Lin YC, Davis RV, Ballew E (1966) The purification and properties of a particulate renal dipeptidase. Biochim Biophys Acta 118: 371-386
    • (1966) Biochim Biophys Acta , vol.118 , pp. 371-386
    • Campbell, B.J.1    Lin, Y.C.2    Davis, R.V.3    Ballew, E.4
  • 6
    • 0021751723 scopus 로고
    • β-Lactamase activity of purified and partially characterized human renal dipeptidase
    • Campbell BJ, Forrester LJ, Zahler WL, Burks M (1984) β-Lactamase activity of purified and partially characterized human renal dipeptidase. J Biol Chem 259:14586-14590
    • (1984) J Biol Chem , vol.259 , pp. 14586-14590
    • Campbell, B.J.1    Forrester, L.J.2    Zahler, W.L.3    Burks, M.4
  • 8
    • 0023930723 scopus 로고
    • Thermostable dipeptidase from Bacillus stearothermophilus: Its purification, characterization, and comparison with aminoacylase
    • Cho HY, Tanizawa K, Tanaka H, Soda K (1988) Thermostable dipeptidase from Bacillus stearothermophilus: Its purification, characterization, and comparison with aminoacylase. J Biochem 103:622-628
    • (1988) J Biochem , vol.103 , pp. 622-628
    • Cho, H.Y.1    Tanizawa, K.2    Tanaka, H.3    Soda, K.4
  • 9
    • 0014429803 scopus 로고
    • Digestive activity of lysosomes
    • Coffey JW, Duve CD (1968) Digestive activity of lysosomes. J Biol Chem 243:3255-3263
    • (1968) J Biol Chem , vol.243 , pp. 3255-3263
    • Coffey, J.W.1    Duve, C.D.2
  • 10
    • 0015350665 scopus 로고
    • Substrate specificity of a highly active dipeptidase purified from monkey small intestine
    • Das M, Radhakrishnan AN (1972) Substrate specificity of a highly active dipeptidase purified from monkey small intestine. Biochem J 128:463-465
    • (1972) Biochem J , vol.128 , pp. 463-465
    • Das, M.1    Radhakrishnan, A.N.2
  • 11
    • 78651153791 scopus 로고
    • Disk electrophoresis. Method and application to human serum proteins
    • Davis BJ (1964) Disk electrophoresis. Method and application to human serum proteins. Ann NY Acad Sci 121:404-427
    • (1964) Ann NY Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 12
    • 0019809411 scopus 로고
    • Modified colorimetric ninhydrin methods for peptidase assay
    • Doi E, Shibata D, Matoba T (1981) Modified colorimetric ninhydrin methods for peptidase assay. Anal Biochem 118:173-189
    • (1981) Anal Biochem , vol.118 , pp. 173-189
    • Doi, E.1    Shibata, D.2    Matoba, T.3
  • 13
    • 0001559155 scopus 로고
    • Contribution of proteolytic enzymes to postmortem changes in muscle
    • Etherington DJ (1984) Contribution of proteolytic enzymes to postmortem changes in muscle. J Anim Sci 55:579-580
    • (1984) J Anim Sci , vol.55 , pp. 579-580
    • Etherington, D.J.1
  • 15
    • 0001874194 scopus 로고
    • Conversion of muscle to meat
    • Bechtel PJ (ed). Academic Press, London
    • Greaser ML (1986) Conversion of muscle to meat. In: Bechtel PJ (ed). Muscle as food. Academic Press, London, pp 37-104
    • (1986) Muscle as Food , pp. 37-104
    • Greaser, M.L.1
  • 16
    • 85008279176 scopus 로고
    • Partial purification and some properties of three kinds of aminopeptidase from carp muscle
    • in Japanese
    • Hara K, Suzumatsu A, Yukawa K, Ishihara T (1987) Partial purification and some properties of three kinds of aminopeptidase from carp muscle. Nippon Suisan Gakkaishi 53:641-647 (in Japanese)
    • (1987) Nippon Suisan Gakkaishi , vol.53 , pp. 641-647
    • Hara, K.1    Suzumatsu, A.2    Yukawa, K.3    Ishihara, T.4
  • 17
    • 0001375881 scopus 로고
    • Purification and characterization of cathepsin B from carp ordinary muscle
    • Hara K, Suzumatsu A, Ishihara T (1988) Purification and characterization of cathepsin B from carp ordinary muscle. Nippon Suisan Gakkaishi 54:1243-1252
    • (1988) Nippon Suisan Gakkaishi , vol.54 , pp. 1243-1252
    • Hara, K.1    Suzumatsu, A.2    Ishihara, T.3
  • 18
  • 19
    • 84998217163 scopus 로고
    • Solubilization and some properties of membrane-bound aminopeptidases of hog small intestinal mucosa
    • in Japanese
    • Hasegawa Y, Kodama O, Akatsuka T (1985) Solubilization and some properties of membrane-bound aminopeptidases of hog small intestinal mucosa. Nippon Nogeikagaku Kaishi 59:397-403 (in Japanese)
    • (1985) Nippon Nogeikagaku Kaishi , vol.59 , pp. 397-403
    • Hasegawa, Y.1    Kodama, O.2    Akatsuka, T.3
  • 20
    • 0015217024 scopus 로고
    • Purification and properties of a mouse ascites tumor dipeptidase, a metalloenzyme
    • Hayman S, Patterson EK (1971) Purification and properties of a mouse ascites tumor dipeptidase, a metalloenzyme. J Biol Chem 246:660-669
    • (1971) J Biol Chem , vol.246 , pp. 660-669
    • Hayman, S.1    Patterson, E.K.2
  • 21
    • 0016209340 scopus 로고
    • The relationship of extrinsic and intrinsic metal ions to the specificity of a dipeptidase from Escherichia coli B
    • Hayman S, Gatmaitan JS, Patterson EK (1974) The relationship of extrinsic and intrinsic metal ions to the specificity of a dipeptidase from Escherichia coli B. Biochemistry 13:4486-4494
    • (1974) Biochemistry , vol.13 , pp. 4486-4494
    • Hayman, S.1    Gatmaitan, J.S.2    Patterson, E.K.3
  • 23
    • 0025169815 scopus 로고
    • Characterization of the glycosylphosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme
    • Hooper NM, Keen JN, Turner AJ (1990) Characterization of the glycosylphosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme. Biochem J 265: 429-433
    • (1990) Biochem J , vol.265 , pp. 429-433
    • Hooper, N.M.1    Keen, J.N.2    Turner, A.J.3
  • 24
    • 0002927661 scopus 로고    scopus 로고
    • Proteolysis of actomyosin by cathepsins B, L, L-like, and X from mackerel (Scomber australasicus)
    • Jiang ST, Lee JJ, Chen HC (1996) Proteolysis of actomyosin by cathepsins B, L, L-like, and X from mackerel (Scomber australasicus). J Agric Food Chem 44:769-773
    • (1996) J Agric Food Chem , vol.44 , pp. 769-773
    • Jiang, S.T.1    Lee, J.J.2    Chen, H.C.3
  • 25
    • 0016325621 scopus 로고
    • Partial purification and characterization of two peptidases from Neurospora crassa
    • Johnson GL, Brown JL (1974) Partial purification and characterization of two peptidases from Neurospora crassa. Biochim Biophys Acta 370: 530-540
    • (1974) Biochim Biophys Acta , vol.370 , pp. 530-540
    • Johnson, G.L.1    Brown, J.L.2
  • 26
    • 0019988899 scopus 로고
    • Glutathione-degrading enzymes of microvillus membranes
    • Kozak EM, Tate SS (1982) Glutathione-degrading enzymes of microvillus membranes. J Biol Chem 257:6322-6327.
    • (1982) J Biol Chem , vol.257 , pp. 6322-6327
    • Kozak, E.M.1    Tate, S.S.2
  • 27
    • 0028274686 scopus 로고
    • Identification and properties of a peptidyl dipeptidase in the housefly, Musca domestica, that resembles mammalian angiotensin-converting enzyme
    • Lamango NS, Isaac RE (1994) Identification and properties of a peptidyl dipeptidase in the housefly, Musca domestica, that resembles mammalian angiotensin-converting enzyme. Biochem J 299:651-657
    • (1994) Biochem J , vol.299 , pp. 651-657
    • Lamango, N.S.1    Isaac, R.E.2
  • 29
    • 84996021762 scopus 로고
    • Studies on fish muscle protease - VIII. On the existence of protease active in neutral pH range
    • Makinodan Y, Ikeda S (1976) Studies on fish muscle protease - VIII. On the existence of protease active in neutral pH range. Bull Jpn Soc Sci Fish 42:665-670
    • (1976) Bull Jpn Soc Sci Fish , vol.42 , pp. 665-670
    • Makinodan, Y.1    Ikeda, S.2
  • 30
    • 0020359766 scopus 로고
    • Renal catabolism of glutathione
    • McIntyre T, Curthoys NP (1982) Renal catabolism of glutathione. J Biol Chem 257:11915-11921
    • (1982) J Biol Chem , vol.257 , pp. 11915-11921
    • McIntyre, T.1    Curthoys, N.P.2
  • 31
    • 49549168250 scopus 로고
    • Studies on a soluble dipeptidase from pig intestinal mucosa
    • Noren O, Sjostrom H, Josefsson L (1973) Studies on a soluble dipeptidase from pig intestinal mucosa. Biochim Biophys Acta 327:446-456
    • (1973) Biochim Biophys Acta , vol.327 , pp. 446-456
    • Noren, O.1    Sjostrom, H.2    Josefsson, L.3
  • 32
    • 0000337085 scopus 로고
    • The enzymology of conditioning
    • Lawrie R (ed). Applied Science Publishers, London
    • Penny IF (1980) The enzymology of conditioning. In: Lawrie R (ed). Developments in meat science-1. Applied Science Publishers, London, pp 406-451
    • (1980) Developments in Meat Science-1 , pp. 406-451
    • Penny, I.F.1
  • 33
    • 0016375398 scopus 로고
    • Characterization of aminopeptidase and one dipeptidase of cytoplasmic soluble fraction from Mycobacterium phlei
    • Plancot MT, Han KK (1974) Characterization of aminopeptidase and one dipeptidase of cytoplasmic soluble fraction from Mycobacterium phlei. J Biochem 75:185-188
    • (1974) J Biochem , vol.75 , pp. 185-188
    • Plancot, M.T.1    Han, K.K.2
  • 35
    • 0017807298 scopus 로고
    • Purification and properties of human kidney dipeptidases
    • Sugiura M, Ito Y, Hirano K, Sawaki S (1978) Purification and properties of human kidney dipeptidases. Biochim Biophys Acta 522:541-550
    • (1978) Biochim Biophys Acta , vol.522 , pp. 541-550
    • Sugiura, M.1    Ito, Y.2    Hirano, K.3    Sawaki, S.4
  • 36
    • 0014690791 scopus 로고
    • The reliability of molecular weight determination by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber K, Osborn M (1969) The reliability of molecular weight determination by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem 244:4406-4412
    • (1969) J Biol Chem , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 37
    • 85008070248 scopus 로고
    • Participation of cathespin L into extensive softening of the muscle of chum salmon caught during spawning migration
    • Yamashita M, Konagaya S (1990) Participation of cathespin L into extensive softening of the muscle of chum salmon caught during spawning migration. Nippon Suisan Gakkaishi 56:1271-1277
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 1271-1277
    • Yamashita, M.1    Konagaya, S.2
  • 38
    • 85010180489 scopus 로고
    • Hydrolytic action of salmon cathepsins B and L to muscle structural proteins in respect of muscle softening
    • Yamashita M, Konagaya S (1991) Hydrolytic action of salmon cathepsins B and L to muscle structural proteins in respect of muscle softening. Nippon Suisan Gakkaishi 57:1917-1922
    • (1991) Nippon Suisan Gakkaishi , vol.57 , pp. 1917-1922
    • Yamashita, M.1    Konagaya, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.