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...

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Bibliographic Details
Published inBioorganicheskaia khimiia Vol. 11; no. 7; p. 895
Main Authors Chashchin, V L, Adamovich, T B, Lapko, V N, Kuprina, N S, Lapko, A G
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.07.1985
Subjects
Adrenal Cortex - enzymology
Amino Acid Sequence
Animals
Cattle
Cholesterol 7-alpha-Hydroxylase - analysis
Chromatography, High Pressure Liquid
Cytochrome P-450 Enzyme System - analysis
Endopeptidases
Hydrolysis
Metalloendopeptidases
Mitochondria - enzymology
Peptide Fragments - analysis
Staphylococcus aureus - enzymology
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Summary: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.
ISSN:0132-3423