earticle

영어

The lectin from Korean and Chines mung bean was finally isolated on sephadex G-100, and then its biochemical properties was measured and compared. The analysis lectin by SDS-PAGE showed two identical bands with molecular weights of 50 and 28 kDa. The lectin agglutinated
rabbit red blood cell treated with trypsin, but did not agglutinated human red blood cells (A, B, AB, O), rat, and native rabbit red blood cell. The optimal temperature and thermal stability of this lectin was at 60℃ and 50℃, respectively. This Korean and Chinese lectin was stable at pH 3.2
and 6.2, respectively. In the presence of denaturant agents, the lectin activity decreases. The hemagglutinating activity was inhibited by Ca2+, Co2+, Cu2+, Fe2+, Mg2+ and Mn2+, and it was inhibited by carbohydrates containing N-acetyl-D-glucosamine. Therefore, there are no differences between the biochemical properties of Korean and Chinese mung bean lectins.