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Physical characterization of a monoamine-sulfating form of phenol sulfotransferase from human platelets

JA Heroux and JA Roth

Department of Pharmacology and Therapeutics, State University of New York at Buffalo, School of Medicine and Biomedical Sciences 14214.

The purification to homogeneity and physical characterization of a monoamine-sulfating form of phenol sulfotransferase (PST) from human platelets is described. DEAE-cellulose chromatography of a 100,000 x g supernatant solution of homogenized human platelets revealed the presence of two peaks of both dopamine- and phenol-sulfating activity, termed M- and P-PST, respectively. The latter dopamine-sulfating form eluting from the ion exchange column, MII-PST, was purified approximately 10,000-fold to electrophoretic homogeneity by Sephacryl S- 200 HR and 3'-phosphoadenosine-5'-phosphate-agarose chromatography. The final specific activity of the enzyme was 930 nmol/min/mg of protein. As determined by the hydrodynamic properties of MII-PST, the native Mr was approximately 69,000. The frictional ratio (f/fo) was estimated to be 1.28, indicating that the enzyme possesses a relatively low degree of asymmetry. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the affinity-purified enzyme revealed the presence of single Mr species of approximately 34,000, suggesting that MII-PST exists as a homodimer in vivo. Isoelectric focusing of purified MII-PST yielded a single protein species with a pl of 4.7. The sulfhydryl- modifying reagent N-ethylmaleimide (50 microM) was found to inactivate MII-PST in a time-dependent manner. This inactivation was totally prevented by saturating concentrations of 3'-phosphoadenosine-5'- phosphosulfate, whereas dopamine bestowed only partial protection to the enzyme. These results suggest that at least one sulfhydryl moiety is present at the active site of MII-PST.

Volume 34, Issue 2, pp. 194-199, 08/01/1988
Copyright © 1988 by American Society for Pharmacology and Experimental Therapeutics




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