Literature DB >> 1189462

Microsomal N-hydroxylation of dibenzylamine.

A H Beckett, G G Gibson.   

Abstract

1. The properties of the rabbit liver microsomal enzyme system(s) catalysing the formation of N,N-dibenzylhydroxylamine as the major metabolite of dibenzylamine have been investigated. 2. The system consists of NADPH- and NADH-dependent components which are differentiated by their different pH optima and sensitivity towards cyanide. 3. The effect of various metabolic inhibitors on the N-oxidation process in vitro are investigated. 4. The N-oxidation of the parent amine was inhibited by CO, SKF 525-A, and inhibitors known to interact with microsomal cytochrome P-450. Phenobarbitone pre-treatment stimulates further metabolism of the hydroxylamine.

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Year:  1975        PMID: 1189462     DOI: 10.3109/00498257509056137

Source DB:  PubMed          Journal:  Xenobiotica        ISSN: 0049-8254            Impact factor:   1.908


  2 in total

1.  Studies on the mechanism of hepatic microsomal N-oxide formation. The role of cytochrome P-450 and mixed-function amine oxidase in the N-oxidation of NN-dimethylaniline.

Authors:  P Hlavica; M Kehl
Journal:  Biochem J       Date:  1977-06-15       Impact factor: 3.857

2.  Studies on the mechanism of hepatic microsomal N-oxide formation. N-oxidation of NN-dimethylaniline by a reconstituted rabbit liver microsomal cytochrome P-448 enzyme system.

Authors:  P Hlavica; S Hülsmann
Journal:  Biochem J       Date:  1979-07-15       Impact factor: 3.857

  2 in total

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