Conservation of functional site structure across different membrane transport protein families

Beuuveriu hsim, pwn in potato dextrose broth and measured their activity by their ability to agglutinate human erythrocytes. The lectins were purified by ion-exchange chromatography and affinity methods to give preparations that gave a single band in SDS-PAGE. Basic characterization has been carried out. The X. polvtnorphu lectin shows specificity for lactose and the B. hassiunu lectin for N-acetyl-Dglucosamine; both lectins have subunit masses of approx. 17 kDa. The N-terminal of each protein was determined. The X. pnlvmrphu lectin shows similarities with the galectin isolated from the fungus Coprims cinereus and is, possibly, a new member of the galectin family. B. hassiaM is insecticidal and it is interesting to note that its lectin has sequence homology with the N-acetyl-D-glucosamine-specific lectin from the fungus