Lectins are proteins or glycoproteins of non-immune origin which bind biospecifically carbohydrates and have reversible agglutinant cell capacity. Species of the genus Bauhinia (Fabaceae) have been used in popular medicine as hypoglycaemic agents. The aim of this work was the purification of B. membranacea leaf lectin (BmeLL) and its immobilization on Sepharose CL-4B (BmeLL-Sepharose) to isolate glycoproteins. A chosen extract (10 %, w/v) was prepared in 0.01 M citrate-phosphate buffer, pH 6.5, containing 0.15 M sodium chloride (selected buffer) by 16 h at 4 ^oC. The extract was treated with ammonium sulphate and a 0-80 % fraction (F0-80%) was used to isolate the lectin since it showed the highest specific hemagglutinating activity (SHA). Chromatography on guar gel column was used to purify BmeLL; the matrix was equilibrated with 0.15 M sodium chloride. Protein elution was performed with 0.02 M sodium hidroxide, pH 11. SDS-PAGE (8.5 %, w/v) revealed pure lectin. HA was obtained at higher titers with rabbit and human erythrocytes; activity was not stimulated in the presence of ions (Ca⁺⁺, Mg⁺⁺). BmeLL showed highest SHA with 0.01 M citrate-phosphate buffer, pH 6.0, containing 0.15 M sodium chloride. A temperature assay revealed that BmeLL was thermostable. Gel filtration chromatographic profile on a Sephacryl S-300 column showed a main protein peak. Casein, fetuin, thyroglobulin, azocasein and asialofetuin abolished lectin activity. BmeLL-Sepharose was efficient to bind avidin and thyroglobulin as well as glycoproteins from hog thyroid. The affinity matrix will be used to isolate and characterize glycoconjugates.