Partial purification and properties of lectin from Rana catesbeiana tadpole.

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Abstract
Lectin from tadpoles of R. catesbeiana was partially purified by gel filtration on Sephadex G-75 followed by successive ion-exchange chromatographies on DEAE-cellulose and CM-cellulose columns. Since intact and enzyme-treated [human] erythrocytes showed no difference in agglutinability by the lectin, a .beta.-galactoside-binding basic protein, this may indicate that the lectin recognizes glycolipid antigens rather than glycoprotein antigens of erythrocytes. In view of the lack of hemagglutinating activity with both acetylated and succinylated lectin, amino groups may be present near the carbohydrate-binding site of the lectin molecule. [Whether the biological role of the frog egg lectin molecule is correlated with the blockage of polyspermy at fertilization or with developmental regulation was investigated.].

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