Literature DB >> 1905668

Polymers of Cu/Zn superoxide dismutase produced by cross-linking with glutaraldehyde.

J M Bond1, J V Bannister, W H Bannister.   

Abstract

Soluble polymers of bovine Cu/Zn superoxide dismutase (EC 1.15.1.1) have been prepared using the homobifunctional cross-linking reagent, glutaraldehyde. A form of the enzyme, a tetramer, with a molecular weight of 64,000 has been purified by gel filtration. The functional properties of the tetramer have been investigated. Reconstitution with copper and zinc was required for full activity. After metal reconstitution, the specific activity of the tetramer was shown to be close to 90% that of the native dimeric enzyme. The serum half-life of the tetramer in rats was found to be increased by a factor of six when compared with native superoxide dismutase. The tissue distribution of the two forms was also found to be different with the tetramer accumulating predominantly in the liver.

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Year:  1991        PMID: 1905668     DOI: 10.3109/10715769109145829

Source DB:  PubMed          Journal:  Free Radic Res Commun        ISSN: 8755-0199


  1 in total

1.  Interaction between dimer interface residues of native and mutated SOD1 protein: a theoretical study.

Authors:  S P Keerthana; P Kolandaivel
Journal:  J Biol Inorg Chem       Date:  2015-01-13       Impact factor: 3.358

  1 in total

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