Abstract
The involvement of microsomal enzymes in the metabolism of the organophosphorus insecticide diethyl p-nitrophenyl phosphorothionate (parathion) by rat liver was studied. The effect of parathion on the activity of NADPH- and NADH-cyto-chrome c reductases in hepatic microsomes isolated from untreated and phenobarbital pretreated rats was determined. The results demonstrate that both NADH- and NADPH-linked (microsomal) electron transport components are involved in the oxidative metabolism of parathion. Phenobarbital pretreatment increased the rate of parathion metabolism. The activity of microsomal NADH-cytochrome c reductase was significantly higher than that of NADPH-cytochrome c reductase. Parathion had an inhibitory effect on both enzymes when applied directly to the microsomal suspension.
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