Abstract
The major hydroxysteroid sulfotransferase found in the livers of female rats has been purified to homogeneity and found to catalyze the transfer of sulfate to any of several hydroxysteroids including dehydroepiandrosterone, estradiol, testosterone, and androstenediol thus forming the corresponding sulfate esters. 3′-Phosphoadenosine 5′-phosphosulfate is the sulfate donor. The reaction is competitively inhibited by both reaction products, i.e., dehydroepiandrosterone sulfate or adenosine 3′,5′-bisphosphate, and also by high concentrations of inorganic phosphate. The enzyme has a molecular weight of approximately 290,000; sodium dodecyl sulfate-gel electrophoresis reveals an apparently single species of 32,000. With standard assay conditions, no activity was observed with the purified enzyme when a phenol, a bile acid, or a hydroxamic acid was used as acceptor for sulfate.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
