Abstract
Lectin from tadpoles of Rana catesbeiana was partially purified by gel filtration on Sephadex G-75 followed by successive ion-exchange chromatographies on diethylaminoethyl (DEAE)-cellulose and carboxymethyl (CM)-cellulose columns. Since intact and enzymetreated erythrocytes showed no difference in agglutinability by the lectin, a β-galactosidebinding 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, it is probable that amino groups are present in the visinity of the carbohydrate-binding site of the lectin molecule.
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