title: [Modification of cytochrome P-450 apoenzyme during its oxidative self-inactivation in a reconstituted mono-oxygenase system].
abstract: The hemoprotein self-inactivation is accompanied by oxidation of all-groups, carbonyl group formation, changes in aggregate state and apoenzyme polymerization. It is probable that heme loss and oxidative modification of apoenzyme is a important step in regulation of P450 decay in cell.
authors.forename: V G
authors.initials: VG
authors.lastname: Zgoda
authors.forename: I I
authors.initials: II
authors.lastname: Karuzina
authors.forename: O V
authors.initials: OV
authors.lastname: Nikitiuk
authors.forename: A I
authors.initials: AI
authors.lastname: Archakov
mesh_terms: D001051:Apoenzymes / Q000037:antagonists & inhibitors*; D001189:Aryl Hydrocarbon Hydroxylases; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D065607:Cytochrome P-450 Enzyme Inhibitors; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence; D013250:Steroid Hydroxylases / Q000037:antagonists & inhibitors*
chemical_list: D001051:Apoenzymes; D065607:Cytochrome P-450 Enzyme Inhibitors; D013250:Steroid Hydroxylases; D001189:Aryl Hydrocarbon Hydroxylases; C050356:steroid 15-alpha-hydroxylase
vernacular_title: Modifikatsiia apofermenta tsitokhroma P450 v protsesse ego okislitel'noĭ samoinaktivatsii v monooksigenaznoĭ rekonstruirovannoĭ sisteme.