Characterization of gastric mucosal mucin receptor

Mucin receptor was isolated from gastric epithelial cell membrane by a procedure involving membrane solubilization with octylglucoside followed by affinity chromatography on Sepharose-bound wheat germ agglutinin. The receptor protein yielded on SDS-PAGE a single 97kDa band and displayed specific affinity, in a concentration-dependent manner, towards the mucin-coated surface. The receptor showed requirement for carbohydrate chains in mucin for binding, as their removal caused a marked (87%) reduction in binding capacity. Scatchard analysis revealed a linear plot with a single class of high affinity binding (Kd = 43.8 nM; Bmax = 140 pmol/mg protein) sites. The results demonstrate for the first time the presence in gastric mucosa of a specific receptor for mucin.