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.
Separopore® macrobeads are larger size (160-250 micron) than average agarose beads that facilitate coupling of cells and organelles and enzymes. Affinity-purified Triticum vulgaris Lectin (WGA) was immobilized on 4% agarose macrobeads with proper configuration and stability of the lectin.