Interactions of styrene and styrene oxide with partially purified cytochrome P-450 and P-448 from rat liver microsomes

Peter Mackenzie, Harri Vainio

Research output: Contribution to journalArticle

Abstract

Styrene and styrene 7,8-oxide were able to bind both to partially purified cytochrome P-450 isolated from phenobarbital (PB)-treated rat liver and to cytochrome P-448 from liver microsomes of 3-methylcholanthrene (3-MC)-treated rats. In the presence of either purified preparation or "fresh" microsomes from PB- or 3-MC-treated animals, styrene produced a characteristic Type I difference spectrum as did styrene 7,8-oxide with "fresh" microsomes from PB rats. In other experiments, the addition of styrene oxide produced spectra which resembled Type I spectra but were somewhat shifted to longer wavelengths. A comparison of the binding parameters for the interaction of styrene or styrene 7,8-oxide with partially purified preparations and "fresh" microsomes indicated that the binding is catalyzed by more than one type of P-450 hemoprotein and that the binding affinity is slightly reduced by the purification procedure. The addition of phosphatidylcholine was unable to restore the binding parameters.

Original languageEnglish
Pages (from-to)183-188
Number of pages6
JournalToxicology Letters
Volume9
Issue number2
DOIs
Publication statusPublished - Oct 1981
Externally publishedYes

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