[Lipid dependence of the activity of cytochrome P-450 from microsomes of rat liver by the phosphatidylcholine transfer protein from bovine liver].
Diatlovitskaia Ev, D Kh Petkova, Bergel'son Ld
Abstract
Diatlovitskaia Ev, D Kh Petkova, Bergel'son Ld
Abstract
The lipid dependence of hydroxylase and demethylase activities of microsomal cytochrome P-450 was studied, using purified phosphatidylcholine transfer protein from bovine liver. In the presence of this protein exogeneous phosphatidylcholine was shown to reactivate cytochrome P-450 inactivated earlier with lysophosphatidylcholine.
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The lipid dependence of hydroxylase and demethylase activities of microsomal cytochrome P-450 was studied, using purified phosphatidylcholine transfer protein from bovine liver. In the presence of this protein exogeneous phosphatidylcholine was shown to reactivate cytochrome P-450 inactivated earlier with lysophosphatidylcholine.
Key concepts: Phosphatidylcholine, Cytochrome, Lysophosphatidylcholine, Microsome, Chemistry, Biochemistry, Cytochrome b5, Microsoma