The sugar moiety of bovine S-antigen.
To obtain insight into the glycoprotein nature of S-antigen (S-Ag), we have investigated the affinity of bovine S-Ag for plant lectins, location of the sugar moiety within the molecule, and incorporation of radiolabelled mannose and glucosamine into S-Ag. It was found (i) that only about 10% of purified S-Ag was bound to concanavalin A (Con A) and wheat germ agglutinin (WGA) columns, (ii) that both concanavalin A and wheat germ agglutinin bound chymotryptic peptides derived from the C-terminal half of S-Ag, and (iii) that radiolabelled D-mannose and D-glucosamine were incorporated into S-Ag and the incorporation was inhibited by tunicamycin, an N-glycosylation inhibitor. 14C-Mannose-labelled S-Ag was identified by affinity chromatography on an anti-S-Ag antibody column. These results support the supposition that only a small population of S-Ag is glycosylated (probably in N-glycosylated form), and the sugar moiety is located in the C-terminal half of the molecule.
Shichi
H
H
Kresge Eye Institute, Department of Ophthalmology, Wayne State University School of Medicine, Detroit, MI 48201.
Koch
K A
KA
D000818:Animals; D000941:Antigens / Q000302:isolation & purification / Q000378:metabolism*; D019393:Arrestin; D002236:Carbohydrate Conformation; D050260:Carbohydrate Metabolism; D002417:Cattle; D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005136:Eye Proteins / Q000302:isolation & purification / Q000378:metabolism*; D005944:Glucosamine / Q000378:metabolism; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D006031:Glycosylation; D008358:Mannose / Q000378:metabolism; D008970:Molecular Weight; D010449:Peptide Mapping; D014909:Wheat Germ Agglutinins / Q000378:metabolism
D000941:Antigens; D019393:Arrestin; D005136:Eye Proteins; D006023:Glycoproteins; D014909:Wheat Germ Agglutinins; D003208:Concanavalin A; D005944:Glucosamine; D008358:Mannose