T. Ara et J. Sekiya, NONRADIOACTIVE ADENOSINE 5'-PHOSPHOSULFATE SULFOTRANSFERASE ASSAY BY COUPLING WITH SULFITE REDUCTASE AND O-ACETYLSERINE(THIOL)LYASE, Bioscience, biotechnology, and biochemistry, 61(4), 1997, pp. 621-624
Adenosine 5'-phosphosulfate (APS) sulfotransferase is thought to be an
enzyme that transfers the sulfo-group of APS to a carrier compound wi
th a thiol group in the assimilatory sulfate reduction pathway of high
er plants. We developed a rapid, non-radioactive assay for APS sulfotr
ansferase. Sulfite released by APS sulfotransferase reaction in the pr
esence of excess dithiothreitol was further converted to cysteine by c
oupling with yeast sulfite reductase and cabbage O-acetylserine(thiol)
lyase. The cysteine thus formed was measured colorimetrically. By this
method, 5 to 300 nmol of sulfite could be assessed. When the method w
as applied to APS sulfotransferase, the enzyme activity was APS-depend
ent with the partially purified enzyme. We could also detect APS sulfo
transferase activity in some higher plants by this method.