|Description:||Superoxide dismutase (SOD) catalyzes the destruction (dismutation) of superoxide free radical ions as follows:SOD2O2- + 2H+ ------> O2 + H2O2The superoxide (O2-) ion is believed to be responsible for lipid peroxidation and peroxidative hemolysis of erythrocytes. The action of superoxide dismutase, therefore, results in protection of the biological integrity of cells and tissues against the harmful effects of superoxide free radicals.|
|Solubility:||Soluble in distilled water or dilute buffer|
|Activity:||3000 U/mg protein|
|Unitdefinition:||That amount of enzyme which, under specified conditions of the assay, will cause a 50% inhibition in the rate of reduction of ferricytochrome C.|
|Assay method:||The method of assay is based on the ability of superoxide dismutase to compete with ferricytochrome C for superoxide anions generated by the xanthine oxidase system. This results in inhibition of the rate of reduction of ferricytochrome C.|
|Introduction:||Superoxide dismutase is widely distributed in both plants and animals. It occurs in high concentrations in brain, liver, heart, erythrocytes and kidney. Three superoxide dismutases have been characterized according to their metal content. The enzyme from bovine and human erythrocytes contains copper and zinc, the one from chicken and rat liver mitochondria contains manganese while the enzyme from E. coli contains iron. Superoxide dismutase from bovine erythrocytes has a molecular weight of 32,500.|
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