The purification of 3 beta-hydroxysteroid sulfotransferase of the hamster epididymis

The purification of a hydroxysteroid sulfotransferase from the cytosolic fraction of the hamster epididymis is described using ammonium sulfate precipitation, gel filtration and PAP agarose affinity chromatography. A purification of 360-fold was achieved and resulted in the isolation of one major protein as evidenced by HPLC and SDS gel-electrophoresis. The "native" enzyme is a dimer of mol. wt 106,000 and is composed of subunits having the same molecular weight.