We describe results which serve as a guide in the selection of protein recovery techniques using two new chromatographic methods based on anion-exchange interaction, i.e., membrane and perfusion chromatographies, which involve enhancement of protein transport by convective now. Bovine serum albumin solution was permeated through a functionalized porous hollow-fiber membrane and a bed charged with functionalized porous (perfusion) beads of identical volume. The pores of the membrane are surrounded by grafted polymer chains immobilizing anion-exchange groups, whereas the throughpores of the beads are surrounded by the diffusive pores at the periphery of which anion-exchange groups are immobilized. An 8-fold increase in throughput of the protein using the porous membrane, 37 mg of BSA/mL/min, was achieved at a low operating pressure of 0.1 MPa, compared to that using the perfusion bed.