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Abstract
Abstract The stoichiometry of the hypoxanthine + uric acid → 2 xanthine reaction, catalysed by chicken liver xanthine dehydrogenase (xanthine: NAD+-oxidoreductase (E.C. 1.2.1.37)), has been determined by u.v. spectrophotometry. The system is adapted to a ping-pong type mechanism; in the proposed reaction sequence, the hypoxanthine is oxidised to xanthine and the reduced form of the enzyme is oxidised by the uric acid, whereby a second xanthine molecule is formed. The reaction product, xanthine, is a non-competitive inhibitor of the enzyme relative to both substrates. Hypoxanthine and excess uric acid are competitive, linear inhibitors of the system.
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