Aqueous extracts from bulb, leaf and root of garlic plant collected at Vanhung-Vanninh, Khanhhoa were examined for hemagglutination activity using native and enzyme-treated different animal and human erythrocytes. All extracts agglutinated at least one type of erythrocytes tested. Activity was detected in extracts from garlic bulb, leaf and root with enzyme-treated rabbit erythrocytes. The hemagglutinins of active species were examined for sugar-binding specificity with various monosaccharides and glycoproteins, pH, temperature stability, and effect of divalent cations using ammonium sulfate precipitates prepared from their extracts. Activity of the hemagglutinins was not inhibited by monosaccharides, but was inhibited by some glycoproteins tested. The inhibition profiles with glycoproteins were different depending on hemagglutinin species, activity of hemagglutinins from garlic leaf and bulb was inhibited by high-mannose type N-glycans, whereas activity of hemagglutinin from garlic root was inhibited by complex type N-glycans, indicating that each part of garlic plant contains different lectins. On the other hand, the activities of hemagglutinins were stable over a wide range of pH and temperature, and independent of the presence of divalent cations. Hemagglutinins from garlic leaf and bulb inhibited the growth of bacterium Enterobacter cloacae, bud did not affect other bacteria examined. These obtained results suggest that the parts of garlic plant may be good sources of usefullectins for many biological applications.