Abstract: Ahstract 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 polyacrylanlide gel clectrophoresis 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 cornponents of erythroagglutinin lectin in large yield and high purity.

Key words: Snow mountain bean lectin