A galactose-binding lectin was isolated in electrophoretically pure form from the seeds of the snake gourd, Trichosanthes anguina, by affinity chromatography on an immobilised lactose column, as well as on a cross-linked Guar Gum column. The lectin agglutinates native erythrocytes of human A, B and 0 phenotypes and of rabbit, rat and mouse. The molecular mass of the lectin, as estimated by Sephadex G-200 gel chromatography, is 49 kDa. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis, after reduction with β-mercaptoethanol, revealed two polypeptide chains linked by disulphide bonds in the lectin molecule. It contains no covalently linked sugars. Amino acid analysis of the lectin revealed a high content of acidic amino acids, relatively lower proportion of basic amino acids and traces of cysteine and methionine. The lectin has good thermal stability, and is inactivated when oxidised by metaperiodate. © 1995 Institute of Experimental Botany, ASCR.
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Dr. Damodaran Vasudevan, Shanavas, K. R., and Elyas, K. K., “Purification and some properties of a lectin from the seeds of Trichosanthes anguina”, Biologia Plantarum, vol. 37, pp. 417-422, 1995.