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ISSN 2063-5346
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PURIFICATION AND CHARACTERIZATION OF A NEW N-ACETYL NEURAMINIC ACID SPECIFIC LECTIN (TcLec) FROM THE MIDGUT GLAND OF THE MILLIPEDE, TRIGONIULUS CORALLINUS

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1*Anitha C 2Basil Rose M.R and 3Viswambari Devi R 4Josephine Priyatharshini C and 5Arokya Glory P.T
» doi: 10.31838/ecb/2023.12.3.075

Abstract

A sialic acid specific lectin with specific affinity for the Gal β13inter-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.

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