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.
Slomiany
B L
BL
Research Center, University of Medicine and Dentistry of New Jersey, Newark 07103-2400.
Piotrowski
J
J
Czajkowski
A
A
Murty
V L
VL
Slomiany
A
A
D000818:Animals; D005753:Gastric Mucosa / Q000378:metabolism*; D066298:In Vitro Techniques; D008297:Male; D009077:Mucins / Q000378:metabolism*; D011869:Radioligand Assay; D051381:Rats; D011956:Receptors, Cell Surface / Q000302:isolation & purification / Q000378:metabolism*
D009077:Mucins; D011956:Receptors, Cell Surface; C085661:mucin receptor