Abstract:Bauhinia variegata lectin(BVL) has been purified from the seed of Bauhinia variegata L. by affinity chromatography on an acidtreated Sepharose 6B column . The hemagglutinating activity of the purified BVL increased 159 times and the activity recovery is 49.0%. The molecular weight is 81 000 and the molecule consists of two identical subunits. Its isoelectric point is 4.95. NacetylDgalactosamine is the most potent inhibitors of BVL. Lactose and galactose can also inhibit the agglutination of rabbit erythocytes by BVL.