雪山豆凝集素红细胞凝集成分的纯化

雪山豆凝集素(SML)经SP-Sephadex C-50和磷酸纤维素离子交换层析分离红血球凝集成分。聚丙烯酰胺凝胶电泳分析和红血球凝集试验为一不均一成分。其中E_2-SML有两条迁移较快的蛋白带,红细胞凝集效价是SML的64倍,是L-SML的512倍。该法制备的红细胞凝集成分具有高的产量和纯度。

PURIFICATION OF ERYTHROAGGLUTININ COMPONENTS FROM SNOW MOUNTAIN BEAN LECTIN

Erythroagglutinin components (E2-SML) are purified from Snow Mountain Bean Lectin (SML) by ion exchange chromatography on SP-Sephadex C-50 and Phosphocellulose column. They are monitored by polyacrylamide gel electrophoresis analysis and hemagglutinating assays. The cathodal proteins (E2 -SML) are potent hemagglutinins with hemagglutination titers 64 and 512 times more potent than SML and L-SML respectively. The methods we used can separate active components of erythroagglutinin lectin in large yield and high purity.