Abstract
A method is given for solubilizing at least one species of cytochrome P.450 from bovine adrenocortical mitochondria. The soluble P.450 supports side-chain cleavage of cholesterol but not 11β-hydroxylation, thus clearly separating these two activities for the first time. Soluble P.450 shows a substrate-induced difference spectrum with both cholesterol and 11-deoxycorticosterone; these difference spectra are opposite in type (peak at 420 nm) to spectra observed when these substrates are added to crude P.450. It is suggested that there are at least two cytochromes P.450 in bovine adrenocortical mitochondria with distinct enzymatic activities namely, side-chain cleavage and 11β-hydroxylation.
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