Lectins are proteins or glycoproteins with a common characteristic of selectivity in the interaction with carbohydrates. These proteins have been immobilized on inert supports and used in glycoprotein purification. The molecular forms of Cratylia mollis seed lectin, Cramoll, recognize glucose/mannose (Cramoll 1, Cramoll 2 and Cramoll 4) or galactose (Cramoll 3) and have been highly purified and characterized. The aim of this work was to evaluate the peroxidase binding capacity to columns of immobilized Cramoll preparations. Columns (1 ml) were equilibrated with 0.15 M NaCl and peroxidase samples were applied  (0.50 mg/ml and 1.24 mg/ml). Adsorbed proteins were eluted with 0.3 M glucose, followed by 1 M NaCl (Cramoll 1,4-Sepharose) or with 0.3 M glucose, followed by 0.3 M galactose and 1 M NaCl (Cramoll 1,2,3-Sepharose). Fractions (2 ml) were collected (flow rate of 10 ml/h) and monitored (A280 nm). Samples of highest absorbances were assembled, liophylized and submitted to polyacrylamide gel electrophoresis (SDS-PAGE). Cramoll 1,4-Sepharose and Cramoll 1,2,3-Sepharose did bind peroxidase; electrophoretic patterns were similar before and after chromatography. Cramoll 1,4-Sepharose was more efficient to adsorb peroxidase. In conclusion, Cramoll affinity matrices bound bioselectively peroxidase and constitute potential tools for glycoprotein purification from species of Brassicaceae family. Supported by: PIBIC/UFPE/CNPq/FACEPE.