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- W2070198081 abstract "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." @default.
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- W2070198081 date "1987-09-01" @default.
- W2070198081 modified "2023-10-17" @default.
- W2070198081 title "Partial purification of cytochrome P450 from rat brain and demonstration of estradiol hydroxylation" @default.
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- W2070198081 doi "https://doi.org/10.1016/s0006-291x(87)80204-8" @default.
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