Enzymatic sulfation of glycolipids by human gastric mucosa

A sulfotransferase activity which catalyzes the transfer of sulfate group from 3'-phosphoadenosine-5'-phosphosulfate to galactosylceramide and triglucosyl monoalkylmonoacylglycerol has been demonstrated in antral and fundic mucosa of normal human stomach. With both types of mucosa maximum activity for sulfation of galactosylceramide was obtained at pH 6.8, whereas the pH optimum for sulfation of triglucosyl monoalkylmonoacylglycerol was 7.8. The reactions were stimulated by the addition of Triton X-100, Mg2+ and F1-. The sulfotransferase activity of fundic mucosa for the synthesis of sulfated glyceroglucolipid was about two times higher than that of antral mucosa, while the enzyme activity for sulfation of glycosphingolipid was similar in both areas of the stomach.