Volume - 13 | Issue-1
Volume - 13 | Issue-1
Volume - 13 | Issue-1
Volume - 13 | Issue-1
Volume - 13 | Issue-1
A sialic acid specific lectin with specific affinity for the Gal β13inter-residue glycosidic linkages of rabbit erythrocytes was purified from the extract of the midgut gland of the rusty millipede, T. corallinus by affinity chromatography using lactoferrin linked cyanogen bromide activated Sepharose-4B and biospecific adsorption using formalinized rabbit erythrocytes. While the lectin purified by biospecific adsorption showed 465-fold augment in specific activity, the affinity purified lectin showed 2925-fold augment in specific activity. The lectin recognized rabbit erythrocytes with greater avidity than the crude agglutinin and was inhibited by lactoferrin with great potency like the crude agglutinin and appeared as a single band with a molecular mass of 76 kDa(named TcLec) on SDS-PAGE. Experiments on hemagglutination with desialylated erythrocytes and hemagglutination inhibition using desialylatedlactoferrin confirmed the sialic acid specificity of the midgut gland lectin.