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• W2041544281 startingPage "1651" @default.
• W2041544281 abstract "Addition of isoniazid (isonicotinic acid hydrazide, INH) to rat liver microsomes produced an immediate decrease in the binding of carbon monoxide to reduced cytochrome P-450. Preincubation of the microsomes with INH in the presence of NADPH produced a further decrease of carbon monoxide binding to cytochrome P-450. The latter decrease of functional cytochrome P-450 was dependent upon NADPH and oxygen and was transitory. Examination of compounds structurally related to INH indicated that both the hydrazine moiety and the aromatic ring were needed to produce both effects. Incubation of microsomes with INH also resulted in gradual increases in absorbance at 449 nm and at 493 nm which also were transitory. Thus, the decreased binding of carbon monoxide to cytochrome P-450 may have occurred concurrently with formation of these spectral intermediates. Microsomal N-demethylation and aniline p-hydroxylation were inhibited by isoniazid. Preincubation of the microsomes with INH and NADPH increased the inhibition. Thus, the decreased availability of cytochrome P-450 as observed may account for the inhibition of the mixed function oxidases by isoniazid." @default.
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• W2041544281 date "1981-06-01" @default.
• W2041544281 modified "2023-09-23" @default.
• W2041544281 title "Mechanism of the inhibitory action of isoniazid on microsomal drug metabolism" @default.
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• W2041544281 doi "https://doi.org/10.1016/0006-2952(81)90393-2" @default.
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