4 výsledky
Adenosin-5'-phosphosulfate (APS) sulfotransferase from higher plants and algae seems to be regulated by adenosine-5'-monophosphate, an endproduct of the APS-sulfotransferase reaction. This was found in crude extracts of Spinacea oleracea L. and Zea mays L. and with partially purified
Active sulfotransferase can be extracted from spinach (Spinacea oleracea L.) leaves (and other higher plants) using a buffer system containing 0.1 M KCl and thiol reagents. This sulfotransferase is labile, it can, however, be stabilized by storage in 70% ammonium sulfate containing 10 mM
Crude extracts of Rhodospirillum rubrum catalyzed the formation of acid-volatile radioactivity from (35S) sulfate, (35S) adenosine-5'-phosphosulfate, and (35S) 3'-phosphoadenosine-5'-phosphosulfate. An enzyme fraction similar to APS-sulfotransferases from plant sources was purified 228-fold from
Adenosine-5'-phosphosulfate (APS) sulfotransferase was purified 25-fold from spinach (Spinacea oleracea L.) leaves by Sephadex-G-200 gel filtration and chromatography on DEAE-cellulose. Enzyme activity was stabilized with 0.05 M Tris-HCl pH 8.0 containing 10 mM mercaptoethanol (ME), 10 mM MgCl2, and