Separation of the cytochromes P-450 in pig kidney mitochondria catalyzing 1 alpha-, 24- and 26-hydroxylations of 25-hydroxyvitamin D3.
The cytochromes P-450 in pig kidney mitochondria catalyzing 1 alpha-, 24- and 26-hydroxylations of 25-hydroxyvitamin D3 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 1 alpha-, 24- and 26-hydroxylations of 25-hydroxyvitamin D3 and provides a basis for further purification and characterization of these enzymes.
Postlind
H
H
Department of Pharmaceutical Biochemistry, University of Uppsala, Sweden.
D015090:25-Hydroxyvitamin D3 1-alpha-Hydroxylase / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D002112:Calcifediol / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006900:Hydroxylation; D007668:Kidney / Q000201:enzymology*; D008928:Mitochondria / Q000201:enzymology; D013250:Steroid Hydroxylases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine
D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; D015090:25-Hydroxyvitamin D3 1-alpha-Hydroxylase; D002112:Calcifediol