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Dextromethorphan O-demethylase activity in rat brain microsomes.

作者信息

Jolivalt C, Minn A, Vincent-Viry M, Galteau M M, Siest G

机构信息

URA CNRS No. 597, Centre du Médicament, Nancy, France.

出版信息

Neurosci Lett. 1995 Feb 24;187(1):65-8. doi: 10.1016/0304-3940(95)11339-x.

DOI:10.1016/0304-3940(95)11339-x
PMID:7617305
Abstract

CYP2D, a genetically variable isoform of cytochrome P450, has been characterized mainly in the liver and the brain of mammals by measurement of debrisoquine hydroxylase activity. Moreover, 'poor debrisoquine metabolizer' phenotype is significantly increased in Parkinson's disease patients. We present here the first demonstration that the activity of the CYP2D isoform can be characterized in rat brain microsomes by the measurement of dextromethorphan O-demethylase capacity. The cerebral formation of dextrorphan, an antagonist of the N-methyl-D-aspartate receptor, was inhibited by the presence of quinidine and N-methyl-4-phenylpyridinium (MPP+), a dopaminergic neurotoxin inducing a chemical parkinsonism in humans.

摘要

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