메뉴 건너뛰기




Volumn 41, Issue 6, 2006, Pages 937-941

Kinetic properties of Cu,Zn-superoxide dismutase as a function of metal content-Order restored

Author keywords

Cytochrome c; Ionic strength; Radiolysis; SOD activity; Superoxide; Superoxide dismutase

Indexed keywords

COPPER COMPLEX; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOCHROME C; EDETIC ACID; PHOSPHATE;

EID: 33747367235     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.05.026     Document Type: Article
Times cited : (48)

References (26)
  • 1
    • 21544438207 scopus 로고    scopus 로고
    • Kinetics properties of Cu,Zn-superoxide dismutase as a function of metal content
    • Michel E., Nauser T., Sutter B., Bounds P.L., and Koppenol W.H. Kinetics properties of Cu,Zn-superoxide dismutase as a function of metal content. Arch. Biochem. Biophys. 439 (2005) 234-240
    • (2005) Arch. Biochem. Biophys. , vol.439 , pp. 234-240
    • Michel, E.1    Nauser, T.2    Sutter, B.3    Bounds, P.L.4    Koppenol, W.H.5
  • 2
    • 0015501473 scopus 로고
    • A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis
    • Klug D., Rabani J., and Fridovich I. A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis. J. Biol. Chem. 247 (1972) 4839-4842
    • (1972) J. Biol. Chem. , vol.247 , pp. 4839-4842
    • Klug, D.1    Rabani, J.2    Fridovich, I.3
  • 4
    • 0015982070 scopus 로고
    • Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis
    • Fielden E.M., Roberts P.B., Bray R.C., Lowe D.J., Mautner G.N., Rotilio G., and Calabrese L. Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis. Biochem. J. 139 (1974) 49-60
    • (1974) Biochem. J. , vol.139 , pp. 49-60
    • Fielden, E.M.1    Roberts, P.B.2    Bray, R.C.3    Lowe, D.J.4    Mautner, G.N.5    Rotilio, G.6    Calabrese, L.7
  • 6
    • 0017473377 scopus 로고
    • A consideration of the effect of added solutes on the activity of bovine superoxide dismutase
    • McAdam M.E. A consideration of the effect of added solutes on the activity of bovine superoxide dismutase. Biochem. J. 161 (1977) 697-699
    • (1977) Biochem. J. , vol.161 , pp. 697-699
    • McAdam, M.E.1
  • 9
    • 0003421978 scopus 로고
    • Critical satbility constants
    • Plenum, New York
    • Smith R.M., and Martell A.M. Critical satbility constants. Inorganic complexes Vol. 4 (1976), Plenum, New York
    • (1976) Inorganic complexes , vol.4
    • Smith, R.M.1    Martell, A.M.2
  • 11
    • 0014691242 scopus 로고
    • Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein)
    • McCord J.M., and Fridovich I. Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244 (1969) 6049-6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 12
    • 0016435588 scopus 로고
    • Effect of ionic strength on the activity of bovine superoxide dismutase
    • Rigo A., Viglino P., Rotilio G., and Tomat R. Effect of ionic strength on the activity of bovine superoxide dismutase. FEBS Lett. 50 (1975) 86-88
    • (1975) FEBS Lett. , vol.50 , pp. 86-88
    • Rigo, A.1    Viglino, P.2    Rotilio, G.3    Tomat, R.4
  • 13
    • 0020357311 scopus 로고
    • Electrostatic interactions in the reaction-mechanism of bovine erythrocyte superoxide-dismutase
    • Cudd A., and Fridovich I. Electrostatic interactions in the reaction-mechanism of bovine erythrocyte superoxide-dismutase. J. Biol. Chem. 257 (1982) 1443-1447
    • (1982) J. Biol. Chem. , vol.257 , pp. 1443-1447
    • Cudd, A.1    Fridovich, I.2
  • 15
    • 0018414062 scopus 로고
    • Bovine erythrocyte superoxide dismutase: diazo coupling, subunit interactions and electrophoretic variants
    • Malinowski D.P., and Fridovich I. Bovine erythrocyte superoxide dismutase: diazo coupling, subunit interactions and electrophoretic variants. Biochemistry 18 (1979) 237-244
    • (1979) Biochemistry , vol.18 , pp. 237-244
    • Malinowski, D.P.1    Fridovich, I.2
  • 16
    • 0023130150 scopus 로고
    • Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions
    • Beyer W.J., and Fridovich I. Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions. Anal. Biochem. 161 (1987) 559-566
    • (1987) Anal. Biochem. , vol.161 , pp. 559-566
    • Beyer, W.J.1    Fridovich, I.2
  • 17
    • 49749184695 scopus 로고
    • Microestimation of succinate and the extinction coefficient of cytochrome c
    • Massey V. Microestimation of succinate and the extinction coefficient of cytochrome c. Biochim. Biophys. Acta 34 (1959) 255-256
    • (1959) Biochim. Biophys. Acta , vol.34 , pp. 255-256
    • Massey, V.1
  • 19
    • 0015935076 scopus 로고
    • Studies on reconstitution of bovine erythrocyte superoxide dismutase.1. Presence of four divalent metal binding sites on apo protein which are different from native sites
    • Fee J.A. Studies on reconstitution of bovine erythrocyte superoxide dismutase.1. Presence of four divalent metal binding sites on apo protein which are different from native sites. Biochim. Biophys. Acta 295 (1973) 87-95
    • (1973) Biochim. Biophys. Acta , vol.295 , pp. 87-95
    • Fee, J.A.1
  • 20
    • 0015935503 scopus 로고
    • On the stability of bovine superoxide dismutase. The effects of metals
    • Forman H.J., and Fridovich I. On the stability of bovine superoxide dismutase. The effects of metals. J. Biol. Chem. 248 (1973) 2645-2649
    • (1973) J. Biol. Chem. , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 21
    • 0000904459 scopus 로고
    • Pulse radiolytic studies on reactions of aqueous superoxide radicals with copper(II) complexes
    • Klugroth D., and Rabani J. Pulse radiolytic studies on reactions of aqueous superoxide radicals with copper(II) complexes. J. Phys. Chem. 80 (1976) 588-591
    • (1976) J. Phys. Chem. , vol.80 , pp. 588-591
    • Klugroth, D.1    Rabani, J.2
  • 22
    • 0020491099 scopus 로고
    • Kinetics and mechanism of the reduction of ferricytochrome-C by the superoxide anion
    • Butler J., Koppenol W.H., and Margoliash E. Kinetics and mechanism of the reduction of ferricytochrome-C by the superoxide anion. J. Biol. Chem. 257 (1982) 747-750
    • (1982) J. Biol. Chem. , vol.257 , pp. 747-750
    • Butler, J.1    Koppenol, W.H.2    Margoliash, E.3
  • 23
    • 0023911964 scopus 로고
    • A critical reevaluation of some assay methods for superoxide dismutase activity
    • Goldstein S., Michel C., Bors W., Saran M., and Czapski G. A critical reevaluation of some assay methods for superoxide dismutase activity. Free Radic. Biol. Med. 4 (1988) 295-303
    • (1988) Free Radic. Biol. Med. , vol.4 , pp. 295-303
    • Goldstein, S.1    Michel, C.2    Bors, W.3    Saran, M.4    Czapski, G.5
  • 24
    • 0031004571 scopus 로고    scopus 로고
    • Lucigenin luminescence as a measure of intracellular superoxide dismutase activity in Escherichia coli
    • Liochev S.I., and Fridovich I. Lucigenin luminescence as a measure of intracellular superoxide dismutase activity in Escherichia coli. Proc. Natl. Acad. Sci. USA 94 (1997) 2891-2896
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2891-2896
    • Liochev, S.I.1    Fridovich, I.2
  • 25
    • 0001298780 scopus 로고
    • Oxygen-dependent mutagenesis in Escherichia-coli lacking superoxide-dismutase
    • Farr S.B., Dari R., and Touati D. Oxygen-dependent mutagenesis in Escherichia-coli lacking superoxide-dismutase. Proc. Natl. Acad. Sci. USA 83 (1986) 8268-8272
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8268-8272
    • Farr, S.B.1    Dari, R.2    Touati, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.