Abstract: Bauhinia variegata lectin（BVL） has been purified from the seed of Bauhinia variegata L. by affinity chromatography on an acidtreated 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. NacetylDgalactosamine is the most potent inhibitors of BVL. Lactose and galactose can also inhibit the agglutination of rabbit erythocytes by BVL.