Heterogeneity of rat liver sulfotransferases.
Sulfotransferases (STs)active on androsterone (AD), cortisol (CS) and 4-nitrophenol (NP) were separated by diethylaminoethyl-cellulose chromatography from cytosolic fractions of female rat liver and were divided into five ST fractions (peaks I-V) with different activities toward three substrates. The precipitates obtained in the 68% of saturation of ammonium sulfate were passed through a Sephadex G-100 column and purified by agarose-hexane adenosine 3',5'-bisphosphate affinity chromatography. AD-ST isoenzyme (peak I) was purified 85-fold, had low CS-ST activity, was devoid of NP-ST activity and appeared to correspond to hydroxysteroid ST 1. Peaks II and V appeared to consist mainly of hydroxysteroid ST and aryl ST, respectively.
D000645:Ammonium Sulfate; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013466:Sulfurtransferases / Q000302:isolation & purification / Q000378:metabolism*
D007527:Isoenzymes; D013466:Sulfurtransferases; D000645:Ammonium Sulfate