Purification and characterization of two major lectins from Vigna mungo (blackgram).

Blackgram (Vigna mungo L. Hepper) seeds contain two galactose-specific lectins, BGL-I and BGL-II. BGL-I was partially purified into two monomeric lectins which were designated as BGL-I-1 (94 kDa) and BGL-I-2 (89 kDa). BGL-II is a monomeric lectin of 83 kDA. The purified lectins were associated with galactosidase activities. BGL-I-1 and BGL-II were copurified with α-galactosidase activity while BGL-I-2 was largely associated with β-galactosidase activity. These lectins agglutinate trypsin treated rabbit erythrocytes, but not the human erythrocytes of A, B or O groups. They were stable between pH 3·5 and 7·5 for their agglutination. The lectins did not show any metalion requirement. They were inactivated at 50°C. The lectin activity was inhibited by D-galactose (0·1 mM). The Scatchard plots of galactose binding to these lectins are nonlinear and biphasic curves indicative of multiple binding sites. The data show that the monomeric lectins have both lectin and galactosidase activities suggestive of a bifunctional protein.

γ-Protein, a sulphur amino acid rich protein from pigeon pea (Cajanus cajan (L.) Millsp.).

A globulin protein comparatively rich in sulphur amino acids has been isolated from the seeds of pigeon pea. This protein termed γ-protein has a sedimentation coefficients of 7S and a molecular weight of about 90,000. Antibodies were raised against pure γ-protein. Using rocket immunoelectrophoresis it was observed that γ-protein was synthesised in the developing seeds, 21 days after flowering.