Sulphation causes heterogeneity of gastric mucins.

The synthesis of mucus glycoprotein in rat stomach was studied in stomach segments, which were pulse-labelled with both [3H]galactose and [35S]sulphate and chased for various times. The radioactive glycoproteins were analyzed by CsCl centrifugation and by agarose gel electrophoresis. After a pulse-labelling for 15 min with [3H]galactose, a possible intermediate with an Mr of 200,000 and a buoyant density of 1.60 g/ml could be demonstrated. Following chase periods of 1 and 4 h, [3H]galactose and [35S]sulphate were present in glycoproteins with a mean buoyant density of 1.50 g/ml. This is clearly different from the main density of glycoproteins isolated from mucosal scrapings (1.46 g/ml). Another difference is the high electrophoretic mobility on gel electrophoretic analysis of newly synthesized glycoproteins compared to that of the major portion of the glycoproteins from mucosal scrapings. When sulphation of glycoproteins was inhibited by sodium chlorate, electrophoretic mobility and buoyant density both decreased. Sodium chlorate had no effect on glycoprotein synthesis nor on glycoprotein secretion. We conclude from our data that the heterogeneity in electrophoretic mobility and buoyant density can be attributed to a different degree of sulphation of the same glycoprotein.