Plant lectins constitute a heterogenous group of proteins differing from each other with respect to their molecular structures, carbohydrate-binding specificies and biological activities. Immobilized lectins have been applied as affinity matrices to isolate and characterize glycoconjugates. A galactose-specific leaf lectin was previously purified from Bauhinia monandra (BmoLL). The aim of this investigation was the immobilization of BmoLL on Sepharose CL-4B (BmoLL-Sepharose) and its evaluation to isolate glycoproteins. The lectin was immobilized on CNBr-activated Sepharose and BmoLL-Sepharose was analyzed for binding of fetal bovine serum glycoproteins, asialofetuin and ovalbumin (0.5 mg) as well as glycoproteins from egg white crude extract and hog thyroid crude homogenate (0.5 ml). Chromatography was performed by application of samples into a 1 ml lectin column, at room temperature; fractions (1 ml) were collected. Unbound material was washed with 0.01 M citrate-phosphate buffer, pH 6.5, containing 0.15 M sodium chloride (selected buffer) until baseline absorbance readings. Adsorbed fractions were eluted with 0.05 M galactose in selected buffer followed by 1 M sodium chloride. No protein peaks were obtained with 0.05 M galactose but, after this previous stage, glycoproteins elution was performed with 1.0 M sodium chloride. BmoLL-Sepharose was efficient to adsorb bioselectively asialofetuin and ovalbumin as well as glycoproteins from fetal bovine serum, egg white and hog thyroid. Thus, the affinity matrix containing BmoLL can be used to isolate glycoconjugates.