[Lipid dependence of cytochrome P-450 activity in rat liver microsomes using lipid exchange proteins].
Diatlovitskaia Ev, Petkova DKh, Lemenovskaia Af, Bergel'son Ld
Abstract
Diatlovitskaia Ev, Petkova DKh, Lemenovskaia Af, Bergel'son Ld
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.
Key concepts: Cytochrome, Microsome, Lysophosphatidylcholine, Phosphatidylcholine, Biochemistry, Chemistry, Microsomal triglyceride transfer protein, Enzyme