Bauhinia purpurea agglutinin or lectin (BPA/BPL) is a tetrameric lectin with a molecular weight of 195,000. Binding appears to be highest for glycoconjugates containing galactosyl (β-1,3)N-acetylgalactosamine structures but oligosaccharides with a terminal α-linked N-acetylgalactosamine can also bind. BPA is lactose-specific and elutes with the sugar lactose. It has specificity for blood groups A, B, O (-SA). Treatment of erythrocytes with neuraminidase or trypsin will increase the agglutination reaction, indicating that the receptor is masked by terminal carbohydrates.
Although binding specificity is similar to that of peanut agglutinin, tissue staining patterns of these two lectins are distinct. Makela's group 2 sugars, particularly N-acetyl-D-galactosamine, are potent inhibitors. The native protein appears to be stable in detergent solution.
Affinity purified Bauhinia purpurea Lectin (BPL/BPA) is immobilized on aminated paramagnetic beads using EDC and stabilized in a buffer to retain maximum activity. These beads are ideal for iP applications to pull down glycoproteins.