The lectin from Bauhinia purpurea: effect of modification of lysine residues on conformation and biological properties.
1993
Balasubramaniam N.K. | Timm D.E. | Neet K.E. | Rao A.G.
Bauhinia purpurea agglutinin (BPA) has been previously characterized as an N-acetylgalactosamine binding protein. The protein has also been demonstrated to possess toxic effects on the European corn borer (ECB), a major insect pest of corn. To understand the role of specific amino acid side chains in the biological and biochemical properties of the protein, we have examined the effect of modification of lysine epsilon-NH2 groups on the conformation and sugar binding properties, as well as the toxicity of BPA toward the com borer. Modification through guanidination retention of positive charge) and carbamylation (conversion to neutral residue) indicated some conformational differences between the native and the modified species, although the sugar binding, hemagglutinating, and toxic properties were indistinguishable. However, succinylation (conversion to negative charge) caused significant changes in the conformation and biological activity of the molecule. Significantly, the deglycosylated form of the protein retained complete toxicity toward the corn borer.
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