Irreversible protein binding of acrylonitrile

Abstract
After i.p. injection of [2,3-14C]acrylonitrile [a toxic industrial chemical] to rats, a significant portion of radioactivity becomes irreversibly attached to proteins of liver, lung, spleen and other tissues. When rat liver microsomes were incubated with [2,3-14C]acrylonitrile, a time-dependent irreversible binding of radioactivity occurred to microsomal proteins. This binding was not dependent on NADPH. A high extent of binding to heat-inactivated microsomes indicated that no enzymic metabolic step was involved. The irreversible binding of [2,3-14C]acrylonitrile to rat liver microsomal protein in vitro was inhibited by thiols (cysteine, glutathione and mercaptoethanol). The greatest inhibitory potency was displayed by dithiocarb (diethyl dithiocarbamate).

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