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Volumn 28, Issue 10, 1996, Pages 1163-1168

Kinetic properties of camel lens ζ-crystallin

Author keywords

DTT; Kinetic mechanism; Lens crystallin; NADPH:quinone oxidoreductase

Indexed keywords

CRYSTALLIN; OXIDOREDUCTASE;

EID: 0030272854     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/1357-2725(96)00048-9     Document Type: Article
Times cited : (3)

References (23)
  • 1
    • 0024356865 scopus 로고
    • Eye lens ζ-crystallin relationships to the family of "Long-chain" Alcohol/polyl dehydrogenases. Protein trimming and conservation of stable parts
    • Borras T., Persson B. and Jornvall H. (1989) Eye lens ζ-crystallin relationships to the family of "Long-chain" Alcohol/polyl dehydrogenases. Protein trimming and conservation of stable parts. Biochemistry 28, 6133-6139.
    • (1989) Biochemistry , vol.28 , pp. 6133-6139
    • Borras, T.1    Persson, B.2    Jornvall, H.3
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-binding
    • Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-binding. Analyt. Biochem. 72, 248-254.
    • (1976) Analyt. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0027466227 scopus 로고
    • Essential sulfhydryl group of malic enzyme from Escherichia coli
    • Chang G. G., Satterlee J. and Hsu R. Y. (1993) Essential sulfhydryl group of malic enzyme from Escherichia coli. J. Prot. Chem. 12, 7-10.
    • (1993) J. Prot. Chem. , vol.12 , pp. 7-10
    • Chang, G.G.1    Satterlee, J.2    Hsu, R.Y.3
  • 4
    • 0027219704 scopus 로고
    • Inhibition of NAD(P)H: Quinone acceptor oxidoreductase by flavones: A structure-activity study
    • Chen S., Hwang J. and Deng P. S. K. (1993) Inhibition of NAD(P)H: quinone acceptor oxidoreductase by flavones: a structure-activity study. Arch. Biochem. Biophys. 302, 72-77.
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 72-77
    • Chen, S.1    Hwang, J.2    Deng, P.S.K.3
  • 6
    • 0023689021 scopus 로고
    • Purification and some properties of camel lens crystallins
    • Duhaiman A. S. (1988) Purification and some properties of camel lens crystallins. Curr. Eye Res. 7, 871-876.
    • (1988) Curr. Eye Res. , vol.7 , pp. 871-876
    • Duhaiman, A.S.1
  • 7
    • 0025081927 scopus 로고
    • Age-dependent variations in the camel lens crystallins
    • Duhaiman A. S. and Ismail M. (1990) Age-dependent variations in the camel lens crystallins. Comp. Biochem. Physiol. 97B, 209-214.
    • (1990) Comp. Biochem. Physiol. , vol.97 B , pp. 209-214
    • Duhaiman, A.S.1    Ismail, M.2
  • 9
    • 0002117840 scopus 로고
    • DT-diaphorase: A historical review
    • Ernster L. (1987) DT-diaphorase: a historical review. Chem. Ser. 27A, 1-13.
    • (1987) Chem. Ser. , vol.27 A , pp. 1-13
    • Ernster, L.1
  • 10
    • 0011877042 scopus 로고
    • The basic equations of enzyme kinetics
    • Edited by Fersht A., Freeman and Company, San Francisco
    • Fersht A. (1985) The basic equations of enzyme kinetics. In Enzyme Structure and Mechanism (Edited by Fersht A.), pp. 389-452, Freeman and Company, San Francisco.
    • (1985) Enzyme Structure and Mechanism , pp. 389-452
    • Fersht, A.1
  • 12
    • 0025743429 scopus 로고
    • Modification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate
    • Gavva S. R., Harris B. G., Weiss P. M. and Cook P. F. (1991) Modification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate. Biochemistry 30, 5764-5769.
    • (1991) Biochemistry , vol.30 , pp. 5764-5769
    • Gavva, S.R.1    Harris, B.G.2    Weiss, P.M.3    Cook, P.F.4
  • 14
    • 0025174965 scopus 로고
    • Association of hereditary cataracts in strain 13/N guinea pigs with mutation of the gene for ζ-crystallin
    • Huang Q. L., Du X. Y., Stone S. H., Amsbaugh D. F., Datiles M. Hu, Hu T. S. and Zigler J. S. Jr. (1990) Association of hereditary cataracts in strain 13/N guinea pigs with mutation of the gene for ζ-crystallin. Exp. Eye Res. 50, 317-325.
    • (1990) Exp. Eye Res. , vol.50 , pp. 317-325
    • Huang, Q.L.1    Du, X.Y.2    Stone, S.H.3    Amsbaugh, D.F.4    Datiles, M.Hu.5    Hu, T.S.6    Zigler J.S., Jr.7
  • 17
    • 0028034204 scopus 로고
    • Oxidation of monohydric phenol substrates by tyrosinase: Effect of dithiothreitol on kinetics
    • Naish-Byfield S., Cooksey C. J. and Riley P. A. (1994) Oxidation of monohydric phenol substrates by tyrosinase: effect of dithiothreitol on kinetics. Biochem. J. 304, 155-162.
    • (1994) Biochem. J. , vol.304 , pp. 155-162
    • Naish-Byfield, S.1    Cooksey, C.J.2    Riley, P.A.3
  • 18
    • 0024520027 scopus 로고
    • Enzyme/crystallins: Gene sharing as an evolutionary strategy
    • Piatigorsky J. and Wistow G. J. (1989) Enzyme/Crystallins: Gene sharing as an evolutionary strategy. Cell 57, 197-199.
    • (1989) Cell , vol.57 , pp. 197-199
    • Piatigorsky, J.1    Wistow, G.J.2
  • 19
    • 0026556950 scopus 로고
    • Identification and characterization of the enzymatic activity of ζ-crystallin from guinea pig lens
    • Rao P. V., Krishna M. and Zigler J. S. Jr. (1992) Identification and characterization of the enzymatic activity of ζ-crystallin from guinea pig lens. J. Biol. Chem. 267, 96-102.
    • (1992) J. Biol. Chem. , vol.267 , pp. 96-102
    • Rao, P.V.1    Krishna, M.2    Zigler J.S., Jr.3
  • 20
    • 0003791209 scopus 로고
    • Steady/state kinetics of multireactant enzymes
    • Edited by Segal I. H., Wiley-International Publications, New York
    • Segal I. H. (1975) Steady/state kinetics of multireactant enzymes. In Enzyme Kinetics (Edited by Segal I. H.), pp. 505-845. Wiley-International Publications, New York.
    • (1975) Enzyme Kinetics , pp. 505-845
    • Segal, I.H.1
  • 21
    • 0021891883 scopus 로고
    • Vitamin K-dependent carboxylase
    • Suttie J. W. (1985) Vitamin K-dependent carboxylase. Ann. Rev. Biochem. 54, 459-477.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 459-477
    • Suttie, J.W.1
  • 22
    • 0019495032 scopus 로고
    • Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase
    • Wermuth B. (1981) Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. 256, 1206-1213.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1206-1213
    • Wermuth, B.1
  • 23
    • 0023917935 scopus 로고
    • Lens crystallins: Evolution and expression of proteins for a highly specialized tissue
    • Wistow G. and Piatigorsky J. (1988) Lens crystallins: evolution and expression of proteins for a highly specialized tissue. Ann. Rev. Biochem. 57, 479-504.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 479-504
    • Wistow, G.1    Piatigorsky, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.