Partial purification and some properties of a lectin from the coelomic fluid of the sea urchin, Toxopneustes pileolus

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We attempted to purify lectin from the coelomic fluid of Toxopneustes pileolus. Coelomic fluid samples induced hemagglutination in rabbit erythrocytes and the proliferation of mouse spleen cells. The samples were shown to contain glycoproteins by SDS-PAGE. Coelomic fluid was fractionated using a Phenyl Sepharose CL-4B column to separate coelomic fluid lectins. Of the fractions recovered, PS-I and PS-II were identified as glycoproteins. Hemagglutinating activity was stronger in the PS-I than PS-II fraction. Therefore, the PS-I fraction was fractionated and purified by gel filtration chromatography using a Superdex 200 column. The PS-PI, PS-PII, and PS-PIII fractions were recovered. The PS-PI fraction showed the strongest hemagglutinating activity among the 3 fractions, and had a heparin-binding property. It showed a nearly single protein band at 960kDa on native PAGE, and it was found to consist of glycoprotein. The PS-PI fraction showed a mitogenic effect on mouse spleen cells from a low concentration. The results of this study suggest that coelomic fluid of Toxopneustes pileolus contains physiologically functional lectins.