title: [Identification of molecular forms of cytochrome P-450 isolated from liver microsomes of rats induced with phenobarbital and 3-methylcholanthrene].
abstract: Eight electrophoretically homogeneous forms of cytochrome P-450 were isolated from liver microsomes of phenobarbital (PB)- and 3-methylcholanthrene (MC)-induced male Wistar rats, using chromatography on 1.8-diaminooctyl-Sepharose, SEAE-Sephacel and hydroxylapatite. These cytochrome forms were compared to those described in literature in terms of their ability to metabolize androstenedione (AD), benzphetamine (BP) and 7-ethoxyresorufin (7-ER). Cytochrome P-450b capable of catalyzing with a high specificity the 16-hydroxylation of AD and N-demethylation of BP, and cytochrome P-450e immunologically related to P-450b but incapable of catalyzing these reactions were isolated from PB-microsomes. Besides, a male-specific cytochrome P-450h catalyzing the 16 alpha-hydroxylation of AD was isolated from PB-microsomes. Cytochrome P-450c possessing a high 7-ER-O-deethylase activity, and a high spin cytochrome P-450d as well as cytochrome P-450a specifically catalyzing the 7 alpha-oxidation of AD were isolated from MC-microsomes. Two forms of cytochrome P-450 isolated from PB-microsomes possessed no such activities. Data from immunochemical analysis suggest that one of these forms can be identified as cytochrome P-450k. It is concluded that the specificity of metabolism and the molecular activity of Wistar rat liver cytochrome P-450 forms are comparable with the corresponding parameters of hemoproteins isolated from other rat species. At the same time, data from metabolic analysis are suggestive of differences in the levels of certain cytochrome P-450 forms, in particular P-450a.
authors.forename: L F
authors.initials: LF
authors.lastname: Guliaeva
authors.forename: O G
authors.initials: OG
authors.lastname: Khatsenko
authors.forename: K E
authors.initials: KE
authors.lastname: Gerasimov
authors.forename: D V
authors.initials: DV
authors.lastname: Mitrofanov
authors.forename: V M
authors.initials: VM
authors.lastname: Mishin
mesh_terms: D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis* / Q000096:biosynthesis / Q000302:isolation & purification; D000072467:Cytochrome P450 Family 2; D004790:Enzyme Induction; D006900:Hydroxylation; D007527:Isoenzymes / Q000032:analysis* / Q000096:biosynthesis / Q000302:isolation & purification; D008297:Male; D008748:Methylcholanthrene / Q000494:pharmacology*; D008862:Microsomes, Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D010634:Phenobarbital / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D039181:Steroid 16-alpha-Hydroxylase
chemical_list: D007527:Isoenzymes; D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System; D001189:Aryl Hydrocarbon Hydroxylases; C450279:CYP2C11 protein, rat; D000072467:Cytochrome P450 Family 2; D039181:Steroid 16-alpha-Hydroxylase; D010634:Phenobarbital
vernacular_title: Identifikatsiia molekuliarnykh form tsitokhroma P-450, izolirovannykh iz mikrosom pecheni krys, indutsirovannykh fenobarbitalom i 3-metilkholantrenom.