Abstract
The copper protein galactose oxidase is now shown to function as a superoxide dismutase as well as an oxidase: At a concentration of about 4 · 10 −7M, it shows its superoxide dismutase activity by a fifty percent inhibition of the reaction of ferricytochrome c with the superoxide anion generated by the xanthine-xanthine oxidase system. The dismutase activity is not due to a minor impurity in the enzyme preparation, as this activity, the galactose oxidase activity, and the protein all have the same mobility on disc gel electrophoresis.
Published Version
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