Abstract
Summary
SQ-18,506, furazolidone, and nitrofurazone are metabolized by at least two enzyme systems in the microsomal and soluble fractions of rat liver. Under anaerobic conditions, the reduction in liver microsomes is mediated by an NADPH-dependent, carbon monoxide insensitive enzyme, presumably NADPH-cytochrome c reductase. Parallel increases in the rates of reduction of the nitrofuran compounds and cytochrome c were noted during the solubilization and partial purification of NADPH-cytochrome c reductase. In the soluble fraction, rat liver xanthine oxidase was able to reduce these compounds. Moreover, this reaction was blocked by allopurinol, an inhibitor of xanthine oxidase, and catalyzed by milk xanthine oxidase.
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