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- W1991350894 abstract "The inhibitory activity of forty-seven 1-, 2-, and 4(5)-substituted imidazoles toward microsomal epoxidation, hydroxylation, and N-demethylation in enzyme preparations from rat liver and armyworm gut has been evaluated. Many of the 1- and 4(5)-substituted compounds are among the most potent inhibitors of microsomal expoxidase and hydroxylase yet reported but are uniformly less active toward N-demethylation. The armyworm gut enzymes are generally more susceptible to inhibition than those from rat liver. Inhibition follows either competitive or mixed type kinetics depending on both the inhibitor and substrate involved. The imidazoles bind powerfully to cytochrome P-450 and yield type II difference spectra in oxidized and NADPH-reduced microsomes. Since spectral dissociation constants (Ks) appear to closely parallel I50 values, the inhibitory activity of the imidazoles is considered to result mainly from their capacity to bind to both cytochrome P-450 and closely related substrate binding sites. Several of the 1-arylimidazoles are potent in vivo synergists of carbaryl against NAIDM insecticide susceptible houseflies." @default.
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- W1991350894 date "1974-09-01" @default.
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- W1991350894 title "Substituted imidazoles as inhibitors of microsomal oxidation and insecticide synergists" @default.
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- W1991350894 doi "https://doi.org/10.1016/0048-3575(74)90113-8" @default.
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