Title : Identification of a reversible component in the in vitro inhibition of rat hepatic cytochrome P450 2B1 by parathion.

Pub. Date : 1995 Feb

PMID : 7853177






3 Functional Relationships(s)
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1 In the present study, two distinct components of the inhibition of the phenobarbital (PB)-inducible P450 2B1 by parathion were characterized. Phenobarbital UDP glucuronosyltransferase family 2 member B17 Rattus norvegicus
2 In the present study, two distinct components of the inhibition of the phenobarbital (PB)-inducible P450 2B1 by parathion were characterized. Phenobarbital UDP glucuronosyltransferase family 2 member B17 Rattus norvegicus
3 At low concentration, parathion was a competitive inhibitor of 2B1-mediated androstenedione 16 beta-hydroxylation (Ki = 0.44 +/- 0.07 microM) and of 7-pentylresorufin O-depentylation (Ki = 0.40 +/- 0.03 microM) in microsomes from PB-pretreated rats and was similarly effective against androstenedione 16 alpha- and 16 beta-hydroxylation catalyzed by purified 2B1. Phenobarbital UDP glucuronosyltransferase family 2 member B17 Rattus norvegicus