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.
D000818:Animals; D011232:Chemical Precipitation; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006224:Cricetinae; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004822:Epididymis / Q000201:enzymology*; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D015238:Sulfotransferases; D013466:Sulfurtransferases / Q000302:isolation & purification*
D046911:Macromolecular Substances; D013466:Sulfurtransferases; D015238:Sulfotransferases; C028152:alcohol sulfotransferase