Literature DB >> 3873950

A new monooxygenase product from 7-ethoxycoumarin and its relation to the O-dealkylation reaction.

B Jung, H Graf, V Ullrich.   

Abstract

The widely used fluorometric microsomal monooxygenase test for 7-ethoxycoumarin O-dealkylation was reinvestigated with regard to other possible hydroxylation products. By HPLC-analysis no beta-hydroxylation of the ethyl group and no 8-hydroxylation could be detected. Only a small percentage of 6-hydroxylation occurred, but as a new major metabolite 7-ethoxy-3-hydroxycoumarin was found in quantities depending on the microsomal preparation used. The ratio of O-dealkylation to 3-hydroxylation varied according to species, induction, buffer and pH, suggesting that different isozymes of cytochrome P450 were involved. The isozyme mainly responsible for 3-hydroxylation exhibited a great dependence on cytochrome b5 as the donor for the second electron. The fluorometric test does not include 3-hydroxylation due to the virtual absence of an emission spectrum above 450 nm.

Entities:  

Mesh:

Substances:

Year:  1985        PMID: 3873950     DOI: 10.1515/bchm3.1985.366.1.23

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN: 0177-3593


  1 in total

1.  Determination of "active" cytochrome P-450 from relaxation kinetics of product formation.

Authors:  U Schröder; H Diehl
Journal:  Eur Biophys J       Date:  1987       Impact factor: 1.733

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.