[Primary structure of 20S,22R-cholesterol-hydroxylating cytochrome P-450 from bovine adrenal cortex mitochondria. III. Primary structure of peptides produced by hydrolysis of the fragment F2 with proteinase from Staphylococcus aureus].
Primary structure of F2 fragment resulting from limited trypsinolysis of the native cytochrome P-450 has been investigated. Hydrolysis of F2 fragment with proteinase from Staphylococcus aureus afforded 18 homogeneous peptides covering the whole polypeptide chain of the fragment. Complete amino acid sequences were established for 16 peptides, two peptides being elucidated partially. The above data in combination with structural study of chymotryptic peptides of cytochrome P-450 and tryptic peptides of F2 fragment led to reconstitution of six peptide blocks of F2 fragment comprising 203 amino acid residues.
D000302:Adrenal Cortex / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002790:Cholesterol 7-alpha-Hydroxylase / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis*; D010450:Endopeptidases; D006868:Hydrolysis; D008666:Metalloendopeptidases; D008928:Mitochondria / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis*; D013211:Staphylococcus aureus / Q000201:enzymology
D010446:Peptide Fragments; D003577:Cytochrome P-450 Enzyme System; D002790:Cholesterol 7-alpha-Hydroxylase; D010450:Endopeptidases; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus
Pervichnaia struktura 20S,22R-kholesteringidroksiliruiushchego tsitokhroma P-450 iz mitokhondriĭ kory nadpochechnikov byka. III. Issledovanie struktury peptidov, poluchennykh pri gidrolize fragmenta F2 proteinazoĭ iz Staphylococcus aureus.