Regular paperRecombinant proteins L and LG: efficient tools for purification of murine immunoglobulin G fragments
Review articleOpen access
R. Vola - No affiliation found
1995/06/23 Full-length article DOI: 10.1016/0378-4347(95)00091-V
Journal: Journal of Chromatography B: Biomedical Sciences and Applications
AbstractIn 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.
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