Four Taro isolectins (I, II, III, IV) were purified by ammonium sulfate, chromatography on CM-celluose and isoelectric focusing. I and IV lectins proved homogeneous by disk polyacrylamid gel electrophoresis and densitometric patterns. But in the presence of urea, IV lectin further dissociated into two different subunits. These lectinis had different hemagglutinating activities and inhibition in their activities after mixed with pepsin particuclary, but not with carbohydrates, heating pH, urea, guanidine, trypsin, pronase and $Ca^{2+}$.