[Localization of tetranitromethane-modified tyrosine residues in domains of cholesterol-hydroxylating cytochrome P-450].
As a continuation of earlier structure-function studies on cholesterol-hydroxylating cytochrome P-450 from the adrenal cortex mitochondria, the present study is concerned with the distribution of tetranitromethane-modified tyrosine residues in the hemo-protein domains. With the aid of thiol-disulfide exchange chromatography and SDS polyacrylamide gel electrophoresis the F1 and F2 fragments of the modified cytochrome P-450 were isolated. Nitrated tyrosine residues were found in the F1 fragment, a heme-containing catalytic domain of the molecule.
D000302:Adrenal Cortex / Q000201:enzymology; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002784:Cholesterol / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006868:Hydrolysis; D006900:Hydroxylation; D066298:In Vitro Techniques; D008697:Methane / Q000031:analogs & derivatives; D008928:Mitochondria / Q000201:enzymology; D013774:Tetranitromethane; D014357:Trypsin; D014443:Tyrosine / Q000378:metabolism*
D014443:Tyrosine; D003577:Cytochrome P-450 Enzyme System; D002784:Cholesterol; D014357:Trypsin; D013774:Tetranitromethane; D008697:Methane
Lokalizatsiia modifitsirovannykh tetranitrometanom ostatkov tirozina v domenakh kholesteringidroksiliruiushchego tsitokhroma P-450.