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[Lipid dependence of cytochrome P-450 activity in rat liver microsomes using lipid exchange proteins].

Diatlovitskaia Ev, Petkova DKh, Lemenovskaia Af, Bergel'son Ld

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Abstract

Modification of membrane lipid composition by lipid exchange proteins was used to study the lipid dependence of cytochrome P-450 activity in rat liver microsomes. The introduction of exogenous lysophosphatidylcholine into microsomal membranes decreased the capacity of cytochrome P-450 to demethylate dimethylaniline and dimethylaminoantipyrine and to hydroxylate aniline. A subsequent introduction of phosphatidylcholine resulted in an almost complete reactivation of the enzyme.

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Modification of membrane lipid composition by lipid exchange proteins was used to study the lipid dependence of cytochrome P-450 activity in rat liver microsomes. The introduction of exogenous lysophosphatidylcholine into microsomal membranes decreased the capacity of cytochrome P-450 to demethylate dimethylaniline and dimethylaminoantipyrine and to hydroxylate aniline. A subsequent introduction of phosphatidylcholine resulted in an almost complete reactivation of the enzyme.

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Available abstract

Modification of membrane lipid composition by lipid exchange proteins was used to study the lipid dependence of cytochrome P-450 activity in rat liver microsomes. The introduction of exogenous lysophosphatidylcholine into microsomal membranes decreased the capacity of cytochrome P-450 to demethylate dimethylaniline and dimethylaminoantipyrine and to hydroxylate aniline. A subsequent introduction of phosphatidylcholine resulted in an almost complete reactivation of the enzyme.

Key concepts: Cytochrome, Microsome, Lysophosphatidylcholine, Phosphatidylcholine, Biochemistry, Chemistry, Microsomal triglyceride transfer protein, Enzyme

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[Lipid dependence of cytochrome P-450 activity in rat liver microsomes using lipid exchange proteins]. — Research Paper | ScholarLens