Purification And Characterization Of Tridax Procumbens Calyx Lectin
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The calyx of the Tridax procumbens L. was found to contain galactose specific lectin. The lectin was purified to homogeneity by affinity chromatography and was found to have molecular weight of 23 kD. The lectin agglutinated papain treated erythrocytes of human blood group ‘A’ ‘B’ and ‘O’, rabbit and other animals. The lectin was stable between pH 4 to 12 for agglutination. The lectin did not require any metal ion for agglutination, but inhibited by Hg++ ions. The agglutination was inhibited by a - D galactose (0.1M) and galactose derivatives. It was found to exhibit a and b - galactosidase activities. The result showed clearly the presence of lectin and galactosidase activities by the same molecule indicating the protein to be bifunctional in nature.
KEYWORDS:Lectin; Tridax procumbens; galactosidase; calyx
