Abstract
The oxidation of either NADH or NADPH by cumene hydroperoxide in rat liver microsomes is described. The Km′ for the hydroperoxide varied with the pyridine nucleotide utilized (NADPH, Km′ = 0.91 mM; NADH, Km′ = 3.3 mM). Carbon monoxide did not inhibit the peroxidase activity although a variety of other agents which interact with cytochrome P 450 did produce inhibitory effects. Moreover, aminotriazole, which stimulated NADPH peroxidase activity, had an inhibitory action on NADPH peroxidase. These various experiments suggest that NADH- and NADPH-dependent peroxidase activity may be mediated by separate components of the microsomal electron transport chain, which may be distinct from but closely interacting with cytochrome P 450.
Published Version
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