Article ID Journal Published Year Pages File Type
10548147 Journal of Chromatography A 2005 11 Pages PDF
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 ∼ 104 M−1) compared well with PpL in binding to immunoglobulins from different classes and sources and, in addition, bound to IgG1 with κ and λ 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 Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
Authors
, , ,