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An artificial protein L for the purification of immunoglobulins and Fab fragments by affinity chromatography

descriptionPublicationkeyboard_double_arrow_right Article 01 Feb 2005Publisher:Elsevier BVJournal:Journal of Chromatography A, volume 1,064, pages 157-167 (issn: 0021-9673,

Authors: A. Cecília A. Roque; M Angela Taipa; Christopher R. Lowe;

doi: 10.1016/j.chroma.2004.11.102

pmid: 15739883

An artificial protein L for the purification of immunoglobulins and Fab fragments by affinity chromatography

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Abstract

The development and characterization of an artificial protein L (PpL) for the affinity purification of antibodies is described. Ligand 8/7, which emerged as the lead from a de novo designed combinatorial library of ligands, inhibits the interaction of PpL with IgG and Fab by competitive ELISA and shows negligible binding to Fc. The ligand 8/7 adsorbent (Ka approximately 10(4) M(-1)) compared well with PpL in binding to immunoglobulins from different classes and sources and, in addition, bound to IgG1 with K and lambda isotypes (92% and 100% of loaded protein) and polyclonal IgG from sheep, cow, goat and chicken. These properties were also reflected in the efficient isolation of immunoglobulins from crude samples.

Related Organizations

Instituto Superior de Espinho
Portugal
University of Cambridge
United Kingdom

Keywords

DNA-Binding Proteins, Immunoglobulin Fab Fragments, Bacterial Proteins, Osmolar Concentration, Immunoglobulins, Enzyme-Linked Immunosorbent Assay, Hydrogen-Ion Concentration, Chromatography, Affinity

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