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

2005; Elsevier BV; Volume: 1064; Issue: 2 Linguagem: Inglês

10.1016/j.chroma.2004.11.102

1873-3778

Ana Cecília A. Roque, M. Ângela Taipa, Christopher R. Lowe,

Glycosylation and Glycoproteins Research

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.