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- W1992382406 abstract "Incubation of [35S]labeled parathion with rat liver microsomes in the presence of an NADPH-generating system leads to the covalent binding of sulfur to the macromolecules of the microsomal membrane. The maximal binding of sulfur to microsomes requires the presence of NADPH, is increased using microsomes from phenobarbital and 3-methyl-cholanthrene-treated animals, and is inhibited by carbon monoxide. The majority, if not all, of the sulfur bound is in a form free of the remainder of the parathion molecule. These findings, coupled with the fact that the apparent Km and Vmax for sulfur binding are not statistically different from the apparent Km and Vmax for metabolism of parathion to paraoxon, indicate the sulfur bound is that released in the mixed-function oxidase-catalyzed metabolism of parathion to paraoxon. Under the conditions of the experiments described in this report, the binding of sulfur to microsomes decreases the concentration of cytochrome P-450 in the microsomes and inhibits slightly the rate of the mixed-function oxidase-catalyzed metabolism of benzphetamine." @default.
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- W1992382406 date "1974-06-01" @default.
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- W1992382406 title "Studies of the binding of sulfur released in the mixed-function oxidase-catalyzed metabolism of diethyl p-nitrophenyl phosphorothionate(parathion) to diethyl p-nitrophenyl phosphate (paraoxon)" @default.
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- W1992382406 doi "https://doi.org/10.1016/0006-2952(74)90400-6" @default.
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