Irreversible protein binding of acrylonitrile.
1. After i.p. injection of [2,3-14C]acrylonitrile to rats, a significant portion of radioactivity becomes irreversibly attached to proteins of liver, lung, spleen and other tissues. 2. 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. 3. The irreversible binding of [2,3-14C]acrylonitrile to rat liver microsomal protein in vitro was inhibited by thiols (cysteine, glutathione, mercaptoethanol). The greatest inhibitory potency was displayed by dithiocarb (diethyl dithiocarbamate).
D000181:Acrylonitrile / Q000378:metabolism*; D000818:Animals; D004050:Ditiocarb / Q000494:pharmacology; D006358:Hot Temperature; D008099:Liver / Q000378:metabolism; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism*; D009570:Nitriles / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D051381:Rats; D013154:Spleen / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D009570:Nitriles; D013438:Sulfhydryl Compounds; D004050:Ditiocarb; D000181:Acrylonitrile