Abstract
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.
Original language | English |
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Pages (from-to) | 1048-1053 |
Number of pages | 6 |
Journal | Journal of Pharmacobio-Dynamics |
Volume | 8 |
Issue number | 12 |
DOIs | |
Publication status | Published - 1985 |
Keywords
- 4-nitrophenol
- androsterone
- cortisol
- isoenzyme
- multiplicity
- rat liver
- sulfotransr erase
ASJC Scopus subject areas
- Pharmacology