Misgurnus anguillicaudatus卵のL-ラムノース結合性レクチンについて

概要

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Loach egg lectin was extracted from the eggs of the fish, Misgurnus 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 50000 mol. wt. 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 μg/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 α-anomers of methyl and phenyl D-galactose were more potent than the corresponding β-anomers. Of the oligosaccharides with a terminal α-linked D-galactose, melibiose, raffinose and stachyose were as potent as α-methyl and phenyl α-galactose. These findings indicate that the specificity of loach egg lectin is different from that of Bandeiraea simplicifolia and Sophora japonica lectin.
公益社団法人日本薬学会の論文
1981-10-25