Rat liver microsomes contain 3α-hydroxysteroid dehydrogenase (HSD) (EC 126.96.36.199) and dihydrodiol dehydrogenase (DHD) (EC 188.8.131.52) activities. The two enzyme activities were solubilized by 10% Triton X-100 or 0.4% sodium deoxycholate. Unlike the cytosolic enzyme (Penning & Talalay (1983) Proc.Natl. Acad. Sci. U.S.A., 80, 4505), the microsomal HSD and DHD activities were not inhibited by indomethacin. Chromatography of the microsomal Triton X-100 extract on Affigel Blue and then on Phenyl-Sepharose gave an HSD preparation containing no detectable (less than 3 - 5%) DHD activity, whereas chromatography of the deoxycholate extract on Phenyl-Sepharose provided a DHD preparation that lacked measurable HSD activity. These results are in sharp contrast to the cytosolic enzyme where both HSD and DHD activities could be copurified to homogeneity (Penning etal. (1984) Biochem. J.222, 601).
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Mar 28 1986|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology