Abstract
We investigated the mechanism of action of uricase, which oxidizes uric acid to allantoin, in the rat. Allantoin may decompose chemically to urea and hydantoin, containing the carbons in positions 2 and 8 of the purine ring, respectively. These carbons are derived by formylation, catalyzed by formyltransferase, in two reactions of de novo synthesis. Since uric acid and allantoin are represented in equivalent amounts in the liver, we expected to find identical incorporation of radioactivity in C2 and C8 of both compounds after administration of 14C-formate. In the case of 14C-allantoin, this was true, but not for 14C-uric acid extracted from rat liver. We interpret these results through a series of experiments and considerations.
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