title: [Molecular organization of cholesterol-hydroxylating cytochrome P-450 from adrenal cortex mitochondria. Chemical modification with bifunctional reagents in the study of oligomeric forms].
abstract: The molecular organization of adrenocortical cytochrome P-450scc has been investigated using chemical modification with bifunctional imidates. The oligomeric organization of cytochrome P-450scc in solution has been shown. The application of dimethyl-3,3'-dithiobispropioimidate and subsequent cleavage of the modified products by reducing agents revealed the presence of two types of intramolecular cross-links: "short" at the distance of 3,0 A between the amino groups of lysine residues and "long" ones at a distance of 11,9 A. The analysis of the products, obtained by limited proteolysis of the oligomeric forms of the cross-linked cytochrome P-450, by two-dimensional electrophoresis has shown that the cross-links are formed between the functional domain (fragment F1) and domain responsible for the interaction with the phospholipid membrane (fragment F2). A model for cytochrome P-450scc molecular organization has been suggested on the basis of the obtained results.
mesh_terms: D000302:Adrenal Cortex / Q000201:enzymology*; D000818:Animals; D002417:Cattle; D002784:Cholesterol / Q000378:metabolism*; D003432:Cross-Linking Reagents; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D066298:In Vitro Techniques; D007700:Kinetics; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D008954:Models, Biological; D013250:Steroid Hydroxylases / Q000378:metabolism*
chemical_list: D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D003577:Cytochrome P-450 Enzyme System; D002784:Cholesterol; D013250:Steroid Hydroxylases
vernacular_title: Molekuliarnaia organizatsiia kholesteringidroksiliruiushchego tsitokhroma P-450 mitokhondriĭ kory nadpochechnikov. Khimicheskaia modifikatsiia bifunktsional'nymi reagentami v issledovanii oligomernykh form.