6533b870fe1ef96bd12cfddd

RESEARCH PRODUCT

Irreversible protein binding of acrylonitrile.

H. M. BoltH. Peter

subject

MaleHot TemperatureHealth Toxicology and MutagenesisSpleenPlasma protein bindingToxicologyBiochemistryDithiocarbchemistry.chemical_compoundNitrilesmedicineAnimalsSulfhydryl CompoundsPharmacologyAcrylonitrileChemistryGeneral MedicineGlutathioneIn vitroRatsmedicine.anatomical_structureBiochemistryLiverMicrosomeMicrosomes LiverAcrylonitrileDitiocarbSpleenCysteineProtein Binding

description

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).

yearjournalcountryeditionlanguage
1981-01-01Xenobiotica; the fate of foreign compounds in biological systems
10.3109/00498258109045271https://pubmed.ncbi.nlm.nih.gov/6261465