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  • Title: [Localization of tetranitromethane-modified tyrosine residues in domains of cholesterol-hydroxylating cytochrome P-450].
    Author: Chashchin VL, Pikuleva IA, Usanov SA, Akhrem AA.
    Journal: Bioorg Khim; 1984 Sep; 10(9):1141-6. PubMed ID: 6508858.
    Abstract:
    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.
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