Aryl sulfotransferase in rat liver: multiplicity and substrate specificity.

Abstract

Rat liver aryl sulfotransferase was purified by chromatography on diethylaminoethyl-cellulose or chromatofocusing and three fractions, referred to by Sekura and Jakoby as I, II and IV, were obtained in the order of their elution, each containing sulfation activity. p-Nitrophenol (PNP) at mM order and beta-naphthol were substrates common to all three fractions, but PNP at microM order and tyramine were substrates only for IV. IV corresponded to the enzyme designated M by Rein et al. and was active with monoamine, as predicted from our previous results with rat liver cytosol. However, the effectiveness of IV in bringing about the sulfation of PNP at mM order was not evident from our previous results. The characteristics of aryl sulfotransferase multiplicity on the basis of thermostability of sulfation activity could not be determined since essentially the characteristics were the same for all three purified fractions. The multiplicity of aryl sulfotransferase purified from rat liver was different from that of human platelets, indicating possible species and/or tissue differences in this enzyme.