Literature DB >> 4346438

Studies on the reconstitution of bovine erythrocyte superoxide dismutase. I. The presence of four divalent metal-binding sites on the apo protein which are different from the native sites.

J A Fee.   

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Year:  1973        PMID： 4346438     DOI： 10.1016/0005-2795(73)90076-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


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  4 in total

1.  The binding of copper ions to copper-free bovine superoxide dismutase. Properties of the protein recombined with increasing amounts of copper ions.

Authors:  A Rigo; M Terenzi; P Viglino; L Calabrese; D Cocco; G Rotilio
Journal:  Biochem J       Date:  1977-01-01       Impact factor: 3.857

2.  Reduction and inactivation of superoxide dismutase by hydrogen peroxide.

Authors:  R C Bray; S A Cockle; E M Fielden; P B Roberts; G Rotilio; L Calabrese
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857

3.  Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis.

Authors:  E M Fielden; P B Roberts; R C Bray; D J Lowe; G N Mautner; G Rotilio; L Calabrese
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857

4.  Regulation of aortic CuZn-superoxide dismutase with copper. Effects in vivo.

Authors:  C T Dameron; E D Harris
Journal:  Biochem J       Date:  1987-12-15       Impact factor: 3.857
  4 in total

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