Bauhinia lectin (BPA/BPL) is a tetramer lectin with a molecular weight of 195,000. Glycoconjugates containing the structure of galactose (-1,3) n-acetylgalactosamine bind best, but oligosaccharides terminally attached to n-acetylgalactosamine can also bind. BPA is lactose specific and can be eluted with lactose. It is specific for blood groups A, B, O (-SA). Treating red blood cells with neuraminidase or trypsin increases agglutination, indicating that the receptor is masked by terminal carbohydrates. Although the binding specificity is similar to peanut lectins, the tissue staining patterns of the two lectins are different. Makela's Group 2 sugars, especially n-acetyl-D-galactosamine, are potent inhibitors. Natural proteins show stability in detergent solutions.
For research use only, not for clinical use.