SULFATION OF HYPERTENSIVE AND HYPOTENSIVE DRUGS BY MONKEY BRAIN PHENOL SULFOTRANSFERASE

The substrate specificity and affinity of two forms of phenol sulfotra nsferase (PST) from Rhesus macaque brain cortex were studied. Catechol amines, their methylated metabolites (normetanephrine, metanephrine) a nd methylated precursor, alpha-methylDOPA, were examined as substrates for both the cationic (PST I) and the anionic (PST II) forms of the e nzyme. Sulfation of hypertensive drugs (phenylephrine, octopamine, met araminol), hypotensive drugs (alpha-methylDOPA, minoxidil), and relate d agents without a free hydroxy group on the benzene ring were also st udied. Results indicated that both PST forms sulfated alpha-methylDOPA and minoxidil, but only PST II transferred the sulfate group to catec holamines and most of the adrenergic agents examined.