Concanavalin A (con A) was immobilized on Mercerized macroporous cellulose membranes and used as a ligand for membrane affinity chromatography. Three activation and immobilization methods involving 2,4,6-trichloro-1,3,5-triazine, glutaraldehyde or diazotization were employed and compared. To obtain information about the effectiveness of the membranes, the adsorptions of ovalbumin and gamma-globulin on the prepared affinity membranes were investigated under a variety of conditions. The prepared affinity membranes were employed for the separation and purification of peroxidase from horseradish and commercial peroxidase, respectively. The separation and purification were monitored by determining the peroxidase activity, using 3,3',5,5-tetramethylbencidine (TMB) as substrate. For the separation from horseradish, a 24.5% recovery and a 142-fold enrichment was achieved; for the purification of a commercial sample, a 71% recovery and a 2.3-fold enrichment was reached.