title: Is wheat germ agglutinin (WGA) a glycosylated protein?
abstract: Lectin isolated from wheat germ was purified by affinity chromatography on ovogel column, recrystallization and gel filtration on Ultrogel AcA 44 column, eluted with borate buffer to eliminate accidental lectin-ligand interaction products. In 87-times purified WGA preparation fucose, xylose, mannose, galactose and glucose were found, amounting 1.5% of lectin mass.
authors.affiliation: Department of General and Organic Chemistry, Medical Academy of Białystok.
authors.forename: D G
authors.initials: DG
authors.lastname: Kisiel
authors.forename: A
authors.initials: A
authors.lastname: Gindzieński
authors.forename: K
authors.initials: K
authors.lastname: Zwierz
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D014909:Wheat Germ Agglutinins / Q000032:analysis*
chemical_list: D014909:Wheat Germ Agglutinins