In vitro covalent binding of cismethrin, bioresmethrin, and their common alcohol to hepatic proteins
When (/sup 14/C)Alcohol-labeled cismethrin, bioresmethrin, and 5-benzyl-3-furylmethyl alcohol (BFA) were incubated with rat liver S 9 homogenates or microsomes, a proportion of the radioactive compounds was covalently bound to proteins. The covalent binding was greater with phenobarbital-pretreated rats, and dependent on a NADPH-generating system. When a S 9 homogenate was used, the bound compounds were two times higher for cismethrin than for bioresmethrin and BFA. Inversely, when microsomes were used more covalent binding occurred with bioresmethrin and BFA than with cismethrin. The inhibition of esterases by tetraethyl pyrophosphate (TEPP) in a S 9 homogenate did not alter the amount of covalent binding to the three compounds whereas malathion inhibited this binding. Treatment of a S 9 homogenate with piperonyl butoxide, however, greatly reduced covalent binding. Covalent binding was inhibited when the microsomes were incubated with carbon monoxide or modified by thermal denaturation. It is suggested that oxidative metabolism was responsible for the covalent binding.
- Research Organization:
- INSERM U 75, CHU Necker-Enfants Malades, Paris, France
- OSTI ID:
- 5558487
- Journal Information:
- Toxicol. Appl. Pharmacol.; (United States), Vol. 77:1
- Country of Publication:
- United States
- Language:
- English
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BIOCHEMICAL REACTION KINETICS
CHEMICAL BONDS
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CARBON MONOXIDE
COMPARATIVE EVALUATIONS
COVALENCE
ENZYME INHIBITORS
ESTERASES
HOMOGENATES
IN VITRO
LIVER
METABOLISM
MICROSOMES
PHENOBARBITAL
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CELL CONSTITUENTS
CENTRAL NERVOUS SYSTEM DEPRESSANTS
CHALCOGENIDES
DIGESTIVE SYSTEM
DRUGS
ENZYMES
GLANDS
HETEROCYCLIC COMPOUNDS
HYDROLASES
HYPNOTICS AND SEDATIVES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
MAMMALS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
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ORGANOIDS
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PESTICIDES
PHOSPHORUS COMPOUNDS
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550201* - Biochemistry- Tracer Techniques