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Xenobiotica
the fate of foreign compounds in biological systems
Volume 18, 1988 - Issue 5
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Original Article

Biophysical and catalytic properties of the phenobarbital p-hydroxylase—a cytochrome P-450 dependent mixed function oxidase

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Pages 545-550 | Received 12 Jun 1987, Accepted 18 Dec 1987, Published online: 30 Sep 2009
 

Abstract

1. A sensitive method to detect and quantify the products of phenobarbital (PB) hydroxylation by model chemical systems and by biological systems has been developed.

2. Chemical model systems hydroxylate PB in the p-position of the phenyl ring and form one or two additional oxidation products, while in vitro and in vivo (bile fistular rats) biological systems hydroxylate PB only in the p-position.

3. Phenobarbital hydroxylation rates in vitro are of the order of 0˙007 nmol/nmol cytochrome P-450 per min. These values are decreased by pretreatment of the rats with inducing doses of phenobarbital.

4. Enzymes catalysing the p-hydroxylation reaction of phenobarbital are localized in the microsomes and have the biophysical and chemical properties that are usually associated with cytochrome P-450-dependent mixed function oxidases.

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