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Reactivity for prostaglandins and inhibition by nonsteridal anti-inflammatory drugs of rabbit liver befunolol reductase.

Befunolol (BF) reductase with 3 alpha-hydroxysteroid dehydrogenase activity, which was purified from rabbit liver, catalyzed the oxidoreduction of prostaglandins, indicating that this enzyme has broad substrate specificities for endogenous substances. BF reductase was strongly inhibited by a variety of nonsteridal anti-inflammatory drugs and then a significant correlation was observed between the logarithms of IC50 (concentration required to produce 50% inhibition of BF reductase activity) values and the maximal daily human doses for nonsteroidal anti-inflammatory drugs. These results suggest that the pharmacological potency of nonsteroidal anti-inflammatory drugs may be predicted from the degree of inhibition of BF reductase by these drugs.