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  • Title: Substrate-binding region of cytochrome P-450SCC (P-450 XIA1). Identification and primary structure of the cholesterol binding region in cytochrome P-450SCC.
    Author: Tsujita M, Ichikawa Y.
    Journal: Biochim Biophys Acta; 1993 Feb 13; 1161(2-3):124-30. PubMed ID: 8431464.
    Abstract:
    Cytochrome P-450SCC (P-450 XIA1) from bovine adrenocortical mitochondria was investigated using a suicide substrate: [14C]methoxychlor. [14C]Methoxychlor irreversibly abolished the activity of the side-chain cleavage enzyme for cholesterol (P-450SCC) and the inactivation was prevented in the presence of cholesterol. The binding of [14C]methoxychlor and cytochrome P-450SCC occurred in a molar ratio of 1:1 and the cholesterol-induced difference spectrum of cytochrome P-450SCC was similar with the methoxychlor-induced difference spectrum. [14C]Methoxychlor-binding peptides were purified from tryptic-digested cytochrome P-450SCC modified with [14C]methoxychlor. Determination of the sequence of the amino-acid residues of a [14C]methoxychlor-binding peptide allowed identification of the peptide comprising the amino-terminal amino-acid residues 8 to 28.
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