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Volumn 63, Issue 4, 1996, Pages 433-441

Evidence for the presence of thioltransferase in the lens

Author keywords

Dethiolation; Oxidative stress; Protein modification; Protein thiol mixed disulfide; Thioltransferase

Indexed keywords

ANIMAL TISSUE; ARTICLE; CATTLE; CONTROLLED STUDY; LENS; NONHUMAN; PRIORITY JOURNAL; SWINE;

EID: 0030273558     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1996.0133     Document Type: Article
Times cited : (56)

References (35)
  • 1
    • 0015947802 scopus 로고
    • Mechanism of action of enzymes catalyzing thiol-disulfide interchange. Thioltransferases rather than transhydrogenase
    • Askelof, P., Axelsson, K., Eriksson, S. and Mannervik, B. (1974). Mechanism of action of enzymes catalyzing thiol-disulfide interchange. Thioltransferases rather than transhydrogenase. FEBS Lett. 38, 263-7.
    • (1974) FEBS Lett. , vol.38 , pp. 263-267
    • Askelof, P.1    Axelsson, K.2    Eriksson, S.3    Mannervik, B.4
  • 2
    • 0017820369 scopus 로고
    • Purification and characterization of cytoplasmic thioltransferase (glutathione: Disulfide oxidoreductase) from rat liver
    • Axelsson, K., Eriksson, S. and Mannervik, B. (1978). Purification and characterization of cytoplasmic thioltransferase (glutathione: disulfide oxidoreductase) from rat liver. Biochemistry 17, 2978-84.
    • (1978) Biochemistry , vol.17 , pp. 2978-2984
    • Axelsson, K.1    Eriksson, S.2    Mannervik, B.3
  • 3
    • 0021321955 scopus 로고
    • A rapid sensitive method for detection of alkaline phosphatase conjugated antibody on western blots
    • Blake, M. S., Johnston, K. H., Russell-Jones, G. J. and Gotschlich, E. C. (1984). A rapid sensitive method for detection of alkaline phosphatase conjugated antibody on western blots. Analyt. Biochem. 136, 175-9.
    • (1984) Analyt. Biochem. , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnston, K.H.2    Russell-Jones, G.J.3    Gotschlich, E.C.4
  • 4
    • 0002468844 scopus 로고
    • Mixed disulfides: Biological functions and increase in oxidative stress
    • (Ed. Sies, H.). Academic Press, New York
    • Brigelius, R. (1985). Mixed disulfides: Biological functions and increase in oxidative stress. In Oxidative stress (Ed. Sies, H.) Pp. 243-72. Academic Press, New York.
    • (1985) Oxidative Stress , pp. 243-272
    • Brigelius, R.1
  • 5
    • 0023277545 scopus 로고
    • A single step method of RNA isolation by acid guanidium thiocyanate phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987). A single step method of RNA isolation by acid guanidium thiocyanate phenol-chloroform extraction. Analyt. Biochem. 162, 156-9.
    • (1987) Analyt. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 6
    • 0022571809 scopus 로고
    • A comparison of protein S-thiolation in heart cells treated with t-butyl hydroperoxide or diamide
    • Collison, M. W., Beilder, D., Grimm, L. M. and Thomas, J. A. (1986). A comparison of protein S-thiolation in heart cells treated with t-butyl hydroperoxide or diamide. Biochim. Biophys. Acta. 885, 58-7.
    • (1986) Biochim. Biophys. Acta. , vol.885 , pp. 58-67
    • Collison, M.W.1    Beilder, D.2    Grimm, L.M.3    Thomas, J.A.4
  • 7
    • 0027282758 scopus 로고
    • 2 exposure on lens morphology and biochemistry
    • 2 exposure on lens morphology and biochemistry. Exp. Eye. Res. 57, 157-67.
    • (1993) Exp. Eye. Res. , vol.57 , pp. 157-167
    • Cui, X.L.1    Lou, M.F.2
  • 8
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA, restriction endonuclease fragments to high specificity
    • Feinberg, A. P. and Vogelstein, B. (1983). A technique for radiolabeling DNA, restriction endonuclease fragments to high specificity. Analyt. Biochem. 132, 6-13.
    • (1983) Analyt. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 9
    • 0023654910 scopus 로고
    • The primary structure of pig liver thioltransferase
    • Gan, Z. R. and Wells, W. W. (1987). The primary structure of pig liver thioltransferase. J. Biol. Chem. 262, 6699-6705.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6699-6705
    • Gan, Z.R.1    Wells, W.W.2
  • 11
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina, S. A. and Mieyal, J. J. (1993). Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32, 3368-76.
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 12
    • 0021440787 scopus 로고
    • Purification and some properties of bovine liver cytosol thioltransferase
    • Hatakeyama, M., Tanimotao, Y. and Mizoguchi, T. (1984). Purification and some properties of bovine liver cytosol thioltransferase. J. Biochem. Tokyo 95, 1811-8.
    • (1984) J. Biochem. Tokyo , vol.95 , pp. 1811-1818
    • Hatakeyama, M.1    Tanimotao, Y.2    Mizoguchi, T.3
  • 13
    • 0017165749 scopus 로고
    • Thiol protein disulphide oxidoreductase
    • Hawkins, H. C. and Freedman, R. B. (1976). Thiol protein disulphide oxidoreductase. Biochem. J. 159, 385-93.
    • (1976) Biochem. J. , vol.159 , pp. 385-393
    • Hawkins, H.C.1    Freedman, R.B.2
  • 14
    • 2042476756 scopus 로고
    • Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione
    • Holmgren, A. (1976). Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc. Natl. Acad. Sci. U.S.A. 73, 2275-9.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 15
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
    • Holmgren, A. (1979). Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J. Biol. Chem. 254, 9113-9.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmeli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. (London) 227, 680-7.
    • (1970) Nature. (London) , vol.227 , pp. 680-687
    • Laemmeli, U.K.1
  • 17
    • 0025353464 scopus 로고
    • The role of protein thiol mixed disulfides in cataractogenesis
    • Lou, M. F., Dickerson, J. E. Jr. and Garadi, R. (1990). The role of protein thiol mixed disulfides in cataractogenesis. Exp. Eye Res. 50, 819-26.
    • (1990) Exp. Eye Res. , vol.50 , pp. 819-826
    • Lou, M.F.1    Dickerson J.E., Jr.2    Garadi, R.3
  • 18
    • 0027087293 scopus 로고
    • Human lens protein-thiol mixed disulfides
    • Lou, M. F. and Dickerson, J. E. Jr. (1992). Human lens protein-thiol mixed disulfides. Exp. Eye Res. 55, 889-96.
    • (1992) Exp. Eye Res. , vol.55 , pp. 889-896
    • Lou, M.F.1    Dickerson J.E., Jr.2
  • 19
    • 0001532252 scopus 로고
    • Recovery of oxidative damage in human lenses
    • Lou, M. F. and Xu, G. T. (1994). Recovery of oxidative damage in human lenses. Invest. Ophthal. Vis. Sci. 35(suppl), 1569.
    • (1994) Invest. Ophthal. Vis. Sci. , vol.35 , Issue.SUPPL. , pp. 1569
    • Lou, M.F.1    Xu, G.T.2
  • 20
    • 0028868929 scopus 로고
    • 2 induced cataract in rat lenses: Distributions and effect of aging
    • 2 induced cataract in rat lenses: distributions and effect of aging. Curr. Eye Res. 14, 951-8.
    • (1995) Curr. Eye Res. , vol.14 , pp. 951-958
    • Lou, M.F.1    Xu, G.T.2    Cui, X.L.3
  • 22
    • 0019492995 scopus 로고
    • Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in CSF proteins
    • Merril, H., Goldman, D., Sedman, S. A. and Ebert, M. H. (1981). Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in CSF proteins. Science 211, 1437-8.
    • (1981) Science , vol.211 , pp. 1437-1438
    • Merril, H.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 23
    • 0025895933 scopus 로고
    • Thioltransferase in human red blood cells: Purification and properties
    • Mieyal, J. J., Starke, D. W., Gravina, S. A. and Hocevar, B. A. (1991). Thioltransferase in human red blood cells: Purification and properties. Biochemistry, 30, 6088-97.
    • (1991) Biochemistry , vol.30 , pp. 6088-6097
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Hocevar, B.A.4
  • 24
    • 0000326249 scopus 로고
    • Glutathionyl specificity of thioltransferase: Mechanistic and physiological implications
    • (Eds Packer, L. and Cadenas, E.). Marcel Dekker Inc., New York, Basel, Hong Kong
    • Mieyal, J. J., Srinivasan, U. and Starke, D.W. (1995). Glutathionyl specificity of thioltransferase: Mechanistic and physiological implications. In Biothiols in health and disease (Eds Packer, L. and Cadenas, E.) Pp. 305-72. Marcel Dekker Inc., New York, Basel, Hong Kong.
    • (1995) Biothiols in Health and Disease , pp. 305-372
    • Mieyal, J.J.1    Srinivasan, U.2    Starke, D.W.3
  • 25
    • 0025993780 scopus 로고
    • A putative glutathione-binding site in T4 glutaredoxin investigated by site-directed mutagenesis
    • Nikkola, M., Gleason, F. K., Saarinen, M., Joelson, T., Bjornberg, O. and Eklund, H. (1991). A putative glutathione-binding site in T4 glutaredoxin investigated by site-directed mutagenesis. J. Biol. Chem. 266, 16105-12.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16105-16112
    • Nikkola, M.1    Gleason, F.K.2    Saarinen, M.3    Joelson, T.4    Bjornberg, O.5    Eklund, H.6
  • 26
    • 0028804668 scopus 로고
    • Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human Grx
    • Padilla, A., Martinez-Galisteo, E., Antonio-Barcena, J., Spyrou, G. and Holmgren, A. (1995). Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human Grx. Eur. J. Biochem. 227, 27-34.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 27-34
    • Padilla, A.1    Martinez-Galisteo, E.2    Antonio-Barcena, J.3    Spyrou, G.4    Holmgren, A.5
  • 27
    • 0000630221 scopus 로고
    • Synthesis and characterization of sodium cysteine S-Sulfate monohydrate
    • Segel, I. and Johnson, M. (1963). Synthesis and characterization of sodium cysteine S-Sulfate monohydrate. Analyt. Biochem. 5, 330-7.
    • (1963) Analyt. Biochem. , vol.5 , pp. 330-337
    • Segel, I.1    Johnson, M.2
  • 30
    • 0002711549 scopus 로고
    • The lens and oxidative stress
    • (Ed. Sies H.). Academic Press, London
    • Spector, A. (1991). The lens and oxidative stress. In: Oxidative stress, oxidants and antioxidants. (Ed. Sies H.) Pp. 529-58. Academic Press, London.
    • (1991) Oxidative Stress, Oxidants and Antioxidants , pp. 529-558
    • Spector, A.1
  • 31
    • 0026563230 scopus 로고
    • Study on human erythrocyte thioltransferase: Comparative characterization with bovine enzyme and its physiological role under oxidative stress
    • Terada, T., Oshida, T., Nishimura, M., Maeda, H., Hara, T., Hosomi, S., Mizoguchi, T. and Nishihara, T. (1992). Study on human erythrocyte thioltransferase: Comparative characterization with bovine enzyme and its physiological role under oxidative stress. J. Biochem. 111, 688-92.
    • (1992) J. Biochem. , vol.111 , pp. 688-692
    • Terada, T.1    Oshida, T.2    Nishimura, M.3    Maeda, H.4    Hara, T.5    Hosomi, S.6    Mizoguchi, T.7    Nishihara, T.8
  • 32
    • 0027272873 scopus 로고
    • Modulation of glutathione S transferase activity by a thiol disulfide exchange reaction and involvement of thioltransferase
    • Terada, T., Maeda, H., Okamota, K., Nishinaka, T., Mizoguchi, T. and Nishihara, T. (1993). Modulation of glutathione S transferase activity by a thiol disulfide exchange reaction and involvement of thioltransferase. Arch. Biochem. Biophys. 300, 495-500.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 495-500
    • Terada, T.1    Maeda, H.2    Okamota, K.3    Nishinaka, T.4    Mizoguchi, T.5    Nishihara, T.6
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from acrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979). Electrophoretic transfer of proteins from acrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 34
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (Glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells, W. W., Xu, D. P., Yang, Y. and Rocque, P. A. (1990). Mammalian thioltransferase (Glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J. Biol. Chem. 265, 15361-4.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 35
    • 0028037601 scopus 로고
    • Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins
    • Yoshitake, S., Nanri, H., Fernando, M. R. and Minakami, S. (1994). Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J. Biochem. 116, 42-6.
    • (1994) J. Biochem. , vol.116 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minakami, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.