[Oxidative modification and inactivation of superoxide dismutase by hypochlorite]

Abstract

The inactivating effect of hypochlorite on Cu, Zn-superoxide dismutase (SOD) from bovine erythrocytes has been studied. According to SDS gel electrophoresis and isoelectric focusing data, oxidation is associated with the degradation of the polypeptide chain, formation of aggregates, and appearance of new isoforms. These protein fractions differ from native SOD by the electric charge and molecular mass but possess a catalytic activity. Modified SOD isoforms occur as a result of intramolecular crosslinking of amino groups and aldehydes which is confirmed by the appearance of fluorescence maxima in the longwave region characteristic of such links. It is assumed that the mechanism of SOD inactivation is coupled to the oxidation of amino acids located outside the active center of the enzyme.