@article{ref1,
title="Substrate-binding region of cytochrome P-450SCC (P-450 XIA1). Identification and primary structure of the cholesterol binding region in cytochrome P-450SCC",
journal="Biochimica et biophysica acta",
year="1993",
author="Tsujita, M. and Ichikawa, Y.",
volume="1161",
number="2-3",
pages="124-130",
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.<p /><p>Language: en</p>",
language="en",
issn="0006-3002",
doi="10.1016/0167-4838(93)90205-6",
url="http://dx.doi.org/10.1016/0167-4838(93)90205-6"
}