Wheat germ agglutinin (WGA) is affinity purified lectin that non-enzymatically binds to N-acetyl-D-glucosamine and sialic acid residues of glycoproteins and glycolipids. This lectin protects Triticum vulgaris from insects, yeast and bacteria. WGA consists of two subunits and has a molecular weight of 36,000. It is an acidic protein and has mitogenic activity toward lymphocytes. It agglutinates erythrocytes and most types of malignant cells. WGA, similar to insulin, enhances the rate of glucose oxidation in isolated fat cells. It inhibits C5a receptor interaction and is used for isolation and fractionation of insulin receptors.
Affinity-purified WGA was immobilized to carboxylated polystyrene beads by covalently coupling with EDC (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride) to ensure proper configuration and stability of the lectin. Polystyrene beads are of durable material, chemically and immunologically inert with a long shelf life. Polystyrene bead columns with immobilized antigen/antibody can be re-used without loss of activity. Coupled polystyrene beads come as a suspension.