Abstract
In the oxidation of hypoxanthine and xanthine by chicken liver xanthine dehydrogenase and bovine liver and milk xanthine oxidase, activation appears at high substrate concentrations. Hypoxanthine concentrations greater than 0.04 mM inhibit the bovine enzyme; concentrations greater than 0.09 mM inhibit the milk enzyme. On the other hand, uric acid is a mixed non-competitive inhibitor of bovine liver xanthine dehydrogenase. The phosphate (Na + or K +) and chloride (Na + or K +) ions do not affect bovine live xanthine oxidase activation, but modify the K and V values.
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