In order to improve antibody purification methods, recombinant proteins L and LG were tested in the purification of murine monoclonal immunoglobulin G (IgG) and its fragments. After affinity constant evaluation in different buffer systems, high-performance affinity chromatographic columns were prepared by coupling the proteins to Affi-prep 10 resin and tested with eight different murine monoclonal antibodies and their fragments of different isotypes. Affinity chromatographic experiments confirmed radioimmunoassay results showing that protein L bound 75% of the tested antibody fragments whereas protein LG had affinity for all the tested fragments. These results demonstrate that protein LG is the most powerful Ig-binding tool so far described.