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Volumn 79, Issue 9, 2010, Pages 960-965

Efficiency of superoxide anions in the inactivation of selected dehydrogenases

Author keywords

Dehydrogenase; Enzyme inactivation; Radiation; Reactive oxygen species; Superoxide anion radical; Xanthine oxidase

Indexed keywords

DEHYDROGENASE; ENZYME INACTIVATION; REACTIVE OXYGEN SPECIES; SUPEROXIDE ANION RADICALS; XANTHINE OXIDASE;

EID: 77953359137     PISSN: 0969806X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.radphyschem.2010.04.001     Document Type: Article
Times cited : (20)

References (28)
  • 1
    • 0014203713 scopus 로고
    • The crystallization and properties of glyceraldehyde-3-phosphate dehydrogenase isolated from rabbit muscle by a simplified procedure
    • Amelunxen R.E., Carr D.O. The crystallization and properties of glyceraldehyde-3-phosphate dehydrogenase isolated from rabbit muscle by a simplified procedure. Biochim. Biophys. Acta. 1967, 132(2):256-259.
    • (1967) Biochim. Biophys. Acta. , vol.132 , Issue.2 , pp. 256-259
    • Amelunxen, R.E.1    Carr, D.O.2
  • 2
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL Workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 3
    • 0016205895 scopus 로고
    • Primary and secondary radicals in the radiation-induced inactivation of yeast alcoholdehydrogenase
    • Badiello R., Tamba M., Quintiliani M. Primary and secondary radicals in the radiation-induced inactivation of yeast alcoholdehydrogenase. Int. J.. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 1974, 26(4):311-319.
    • (1974) Int. J.. Radiat. Biol. Relat. Stud. Phys. Chem. Med. , vol.26 , Issue.4 , pp. 311-319
    • Badiello, R.1    Tamba, M.2    Quintiliani, M.3
  • 4
    • 0015898834 scopus 로고
    • Molecular properties of lactic dehydrogenase under the conditions of the enzymatic test. Sedimentation analysis and gel filtration in the microgram and nanogram range
    • Bartholmes P., Durchschlag H., Jaenicke R. Molecular properties of lactic dehydrogenase under the conditions of the enzymatic test. Sedimentation analysis and gel filtration in the microgram and nanogram range. Eur. J. Biochem. 1973, 39:101-108.
    • (1973) Eur. J. Biochem. , vol.39 , pp. 101-108
    • Bartholmes, P.1    Durchschlag, H.2    Jaenicke, R.3
  • 5
    • 0001954441 scopus 로고
    • Superoxide and hydroxyl radical chemistry in aqueous solutions
    • Blackie Academic & Professional, London, C.S. Foote, J.S. Valentine, A. Greenberg, J.F. Liebman (Eds.)
    • Bielski B.H.J., Cabelli D.E. Superoxide and hydroxyl radical chemistry in aqueous solutions. Active Oxygens in Chemistry 1995, 66-104. Blackie Academic & Professional, London. C.S. Foote, J.S. Valentine, A. Greenberg, J.F. Liebman (Eds.).
    • (1995) Active Oxygens in Chemistry , pp. 66-104
    • Bielski, B.H.J.1    Cabelli, D.E.2
  • 8
    • 0017175685 scopus 로고
    • Free radical inactivation of lactate dehydrogenase
    • Int. J. Radiat. Biol.
    • Buchanan, J.B., Armstrong, D.A., 1976. Free radical inactivation of lactate dehydrogenase. Int. J. Radiat. Biol. 30(2), 115-127.
    • (1976) , vol.30 , Issue.2 , pp. 115-127
    • Buchanan, J.B.1    Armstrong, D.A.2
  • 9
    • 0014603264 scopus 로고
    • Yeast alcohol dehydrogenase: SH groups, disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups
    • Buhner M., Sund H. Yeast alcohol dehydrogenase: SH groups, disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups. Eur. J. Biochem. 1969, 11:73-79.
    • (1969) Eur. J. Biochem. , vol.11 , pp. 73-79
    • Buhner, M.1    Sund, H.2
  • 12
    • 63049096113 scopus 로고    scopus 로고
    • The role of proteins in biological damage induced by oxidative stress
    • J. Pietzsch (Ed.)
    • Gebicki J.M. The role of proteins in biological damage induced by oxidative stress. Protein Oxidation and Disease, Research Signpost 2006, 7-38. J. Pietzsch (Ed.).
    • (2006) Protein Oxidation and Disease, Research Signpost , pp. 7-38
    • Gebicki, J.M.1
  • 13
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling
    • Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 1997, 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 14
    • 0028401625 scopus 로고
    • Radiation inactivation of bovine intestinal alkaline phosphatase
    • Hasan N.M., McCall P.R., Moore J.S., Power D.M. Radiation inactivation of bovine intestinal alkaline phosphatase. Radiat. Phys. Chem. 1994, 43(3):205-305.
    • (1994) Radiat. Phys. Chem. , vol.43 , Issue.3 , pp. 205-305
    • Hasan, N.M.1    McCall, P.R.2    Moore, J.S.3    Power, D.M.4
  • 15
    • 0034282214 scopus 로고    scopus 로고
    • How should xanthine oxidase-generated superoxide yields be measured?
    • Hodges G.R., Young M.J., Paul T., Ingold K.U. How should xanthine oxidase-generated superoxide yields be measured?. Free Radical Biol. Med. 2000, 29(5):434-441.
    • (2000) Free Radical Biol. Med. , vol.29 , Issue.5 , pp. 434-441
    • Hodges, G.R.1    Young, M.J.2    Paul, T.3    Ingold, K.U.4
  • 16
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of annotated three-dimensional protein structure homology models
    • Kopp J., Schwede T. The SWISS-MODEL repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res. 2004, 32:D230-D234.
    • (2004) Nucleic Acids Res. , vol.32
    • Kopp, J.1    Schwede, T.2
  • 17
    • 0030594816 scopus 로고    scopus 로고
    • Methods for the separation of lactate dehydrogenases and clinical significance of the enzyme
    • Kopperschlager G., Kirchberger J. Methods for the separation of lactate dehydrogenases and clinical significance of the enzyme. J. Chromatogr. B Biomed. Appl. 1996, 684(1-2):25-49.
    • (1996) J. Chromatogr. B Biomed. Appl. , vol.684 , Issue.1-2 , pp. 25-49
    • Kopperschlager, G.1    Kirchberger, J.2
  • 18
    • 36749009094 scopus 로고    scopus 로고
    • Inactivation of chosen dehydrogenases by the products of water radiolysis and secondary albumin and haemoglobin radicals
    • Kowalczyk A., Serafin E., Puchała M. Inactivation of chosen dehydrogenases by the products of water radiolysis and secondary albumin and haemoglobin radicals. Int. J. Radiat. Biol. 2008, 84(1):15-22.
    • (2008) Int. J. Radiat. Biol. , vol.84 , Issue.1 , pp. 15-22
    • Kowalczyk, A.1    Serafin, E.2    Puchała, M.3
  • 20
    • 0013470674 scopus 로고
    • The content and action of diphosphopyridine nucleotide in triosephosphate dehydrogenase
    • Murdock A., Koeppe O. The content and action of diphosphopyridine nucleotide in triosephosphate dehydrogenase. J. Biol. Chem. 1964, 239:1983-1988.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1983-1988
    • Murdock, A.1    Koeppe, O.2
  • 23
    • 0029001135 scopus 로고
    • Radiation-induced inactivation of enzymes-a review
    • Saha A., Mandal P.C., Bhattacharyya S.N. Radiation-induced inactivation of enzymes-a review. Radiat. Phys. Chem. 1995, 46(1):123-145.
    • (1995) Radiat. Phys. Chem. , vol.46 , Issue.1 , pp. 123-145
    • Saha, A.1    Mandal, P.C.2    Bhattacharyya, S.N.3
  • 24
    • 0344413762 scopus 로고    scopus 로고
    • Oxygen effect in the radiolysis of proteins: V. Histones
    • Schüssler H., Puchala M. Oxygen effect in the radiolysis of proteins: V. Histones. Radiat. Phys. Chem. 2004, 69:45-53.
    • (2004) Radiat. Phys. Chem. , vol.69 , pp. 45-53
    • Schüssler, H.1    Puchala, M.2
  • 25
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 2003, 31:3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 26
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover M.A. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta 1999, 1432(2):159-184.
    • (1999) Biochim. Biophys. Acta , vol.1432 , Issue.2 , pp. 159-184
    • Sirover, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.