Involvement of hepatic mixed function oxidase enzyme system in the oxidative metabolism of methanol.

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Abstract
Methanol is oxidized by liver alcohol dehydrogenase (ADH) and catalase enzymes. This primary alcohol is also metabolized by rat liver mixed function oxidase (MFO) induced by phenobarbital. Comparative studies on the oxidation of methanol and N-demethylation of benzphetamine by MFO reveal that SKF 525-A [2-diethylaminoethyl 2,2-diphenylvalerate hydrochloride] inhibits both reactions, whereas aminotriazole, a known inhibitor of catalase, abolishes the activity of microsomal methanol oxidase with no effect on N-demethylase. While disulfiram depresses N-demethylase activity, pyrazole and cyanide have little or no effect on the microsomal enzyme activity. Although ethanol appears to be a competitive inhibitor of microsomal methanol oxidase it is a poor inhibitor of this enzyme system.

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