Partial purification of cytochrome P450 from rat brain and demonstration of estradiol hydroxylation.
Cytochrome P450 was partially purified from brain microsomes of untreated rats. A difference spectrum of the dithionite-reduced CO-complex of the purified P450 showed essentially the hemeprotein absorbing exclusively at 449 nm. The purified brain P450 was able to catalyze estradiol (E2) hydroxylation leading to the formation of 6 alpha- and 6 beta-hydroxy(OH)E2, 4-OHE2, estrone, 6-oxoE2, 2-OHE2, 15 alpha-OHE2 and estriol. These results demonstrate that rat brain P450 is active in estradiol hydroxylation.
Sugita
O
O
Rockefeller University Hospital, New York, N.Y. 10021.
Miyairi
S
S
Sassa
S
S
Kappas
A
A
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002845:Chromatography; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification* / Q000378:metabolism; D004958:Estradiol / Q000378:metabolism*; D006900:Hydroxylation; D008861:Microsomes / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D051381:Rats
D004958:Estradiol; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases