An L-Rhamnose-Binding Lectin in the Eggs of Misgurnus anguillicaudatus

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Abstract
Loach egg lectin was extracted from the eggs of the fish, M. anguillicaudatus and purified by ion exchange chromatography on DEAE- and CM-cellulose, and affinity chromatography on a column by using L-rhamnose coupled to epoxy-activated Sepharose 6B. The lectin was eluated from the affinity column with L-rhamnose. The lectin purified by affinity chromatography was shown to be homogenous by polyacrylamide gel electrophoresis and identified as a glycoprotein of 5000 MW with an isoelectric point of pH 6.6. This lectin has potent agglutinating activity towards human B type erythrocytes as well as Ehrlich ascites tumor cells and ascites hepatoma, AH 109 A cells and exhibited the agglutinability at a concentration of 1 .mu.g/0.05 ml. The agglutinating activity was inhibited best by L-rhamnose, L-mannose and L-lyxose but suitably by D-galactose, D-fucose and L-arabinose, and other monosaccharides failed to inhibit its agglutinating reaction. Among the glycosides of D-galactose tested, the .alpha.-anomers of methyl and phenyl D-galactose were more potent than the corresponding .beta.-anomers. Of the oligosaccharides with a terminal .alpha.-linked D-galactose, melibiose, raffinose and stachyose were as potent as .alpha.-methyl and phenyl .alpha.-galactose. The specificity of loach egg lectin is different from that of Bandeiraea simplicifolia and Sophora japonica lectin.

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