Abstract
Pig kidney mitochondria were found to catalyze the formation of 26-hydroxycholesterol, an inhibitor of cholesterol biosynthesis. The cholesterol 26-hydroxylase was purified 600-fold. It was present in a mitochondrial enzyme fraction enriched in cytochrome P-450. The cytochrome P-450 fraction required NADPH, mitochondrial ferredoxin and ferredoxin reductase for 26-hydroxylase activity. The mitochondria and the purified 26-hydroxylase preparation also catalyzed 26-hydroxylation of 5β-cholestane-3α, 7α, 12α-triol, an intermediate in cholic acid biosynthesis, and of 25-hydroxyvitamin D 3. The role of extra-hepatic formation of 26-hydroxycholesterol is discussed.
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