Phenol sulphotransferase: purification and characterization of the rat kidney and stomach enzymes.
3'-Phosphoadenosine-5'-phosphosulphate-dependent enzymes that catalyse sulphation of p-nitrophenol have been purified from rat kidney and stomach mucosa by affinity chromatography on the p-hydroxyphenylacetic acid-agarose conjugate, by chromatography on DEAE-cellulose and Sephadex G-100. The phenol sulphotransferase (PST) from rat kidney had Mr of 69 000 and that of the stomach enzyme was 32 000. With p-nitrophenol as the sulphate acceptor, the pH optima were 6.4 for the stomach PST and 5.4 and 6.6 for the kidney enzyme. Both enzymes were inhibited by 2,6-dichloro-4-nitrophenol and phenylglyoxal, an arginine specific modifying reagent. Both enzymes readily sulphated p-nitrophenol, 2-naphthol, 1-naphthol and salicylamide and did not act on biogenic amines (e.g. epinephrine, norepinephrine, dopamine, serotonin), acid metabolites of catecholamines (e.g. 3,4-dihydroxyphenylacetic acid, homovanillic acid), and O-methylated metabolites of catecholamines. Only the stomach enzyme sulphated such catecholamine metabolites as homovanillic alcohol and 3-methoxy-4-hydroxyphenylglycol. In contrast to the brain enzyme, but similarly to the liver enzyme, the kidney and stomach phenol sulphotransferases appear to sulphate exogenous phenolic substrates in preference to potential endogenous substrates.
D000818:Animals; D015239:Arylsulfotransferase; D005753:Gastric Mucosa / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013466:Sulfurtransferases / Q000302:isolation & purification* / Q000378:metabolism; D014018:Tissue Distribution
D013466:Sulfurtransferases; D015239:Arylsulfotransferase