Abstract
The cytochromes P-450 in pig kidney mitochondria catalyzing 1α-, 24- and 26-hydroxylations of 25-hydroxyvitamin D 3 have been separated. The cytochrome P-450 fractions required NADPH, mitochondrial ferredoxin and ferredoxin reductase for catalytic activity. The present report demonstrates that different forms of cytochrome P-450 are involved in 1α-, 24- and 26-hydroxylations of 25-hydroxyvitamin D 3 and provides a basis for further purification and characterization of these enzymes.
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