Partial purification of cytochrome P450 from rat brain and demonstration of estradiol hydroxylation

Biochem Biophys Res Commun. 1987 Sep 30;147(3):1245-50. doi: 10.1016/s0006-291x(87)80204-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Brain / enzymology*
  • Chromatography
  • Cytochrome P-450 Enzyme System / isolation & purification*
  • Cytochrome P-450 Enzyme System / metabolism
  • Estradiol / metabolism*
  • Hydroxylation
  • Microsomes / enzymology
  • Mixed Function Oxygenases / metabolism*
  • Rats


  • Estradiol
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases