6533b7d7fe1ef96bd12684e0

RESEARCH PRODUCT

Enzymic control of irreversible binding of metabolically activated benzo(a)pyrene in perfused rat liver by monooxygenase activity.

G. F. KahlRegine KahlE. KlausH. G. Jonen

subject

MaleHealth Toxicology and MutagenesisIn Vitro TechniquesToxicologychemistry.chemical_compoundBenzopyrene HydroxylasemedicineAnimalsBenzopyrene HydroxylaseFlavonoidsMetyraponeRNAGeneral MedicineDNARatsBiochemistrychemistryBenzo(a)pyreneLiverPhenobarbitalPyreneRNAPhenobarbitalAryl Hydrocarbon HydroxylasesPerfusionDNAmedicine.drugProtein Binding

description

Addition of [3H]-benzo(a)pyrene to the perfusion medium of isolated rat livers results in irreversible binding of radioactivity to DNA, RNA and protein. Binding to DNA accounted for about 0.1% of the total radioactivity which was bound in livers from animals treated with oil or saline and was increased by a factor of 3–5 after pretreatment of the animals with β-naphthoflavone or with phenobarbital. When the inhibitiors of monooygenase activity, α-naphthoflavone or metyrapone, were present in the perfusion medium, irreversible binding was reduced in livers from both β-naphthoflavone- and phenobarbital-pretreated animals, irrespective of the inhibitor used.

yearjournalcountryeditionlanguage
1977-12-30Archives of toxicology
10.1007/bf00343282https://pubmed.ncbi.nlm.nih.gov/579978