@inbook {558,
	title = {Rationally designed ligands for use in Affinity Chromatography: An artificial Protein L},
	booktitle = {Affinity Chromatography: Methods and Protocols},
	year = {2007},
	pages = {93-110},
	publisher = {Humana Press Inc.},
	organization = {Humana Press Inc.},
	address = {U.S.A.},
	abstract = {<p>Synthetic affinity ligands can circumvent the drawbacks of natural immunoglobulin (Ig)-binding proteins by imparting resistance to chemical and biochemical degradation and to in situ sterilization, as well as ease and low cost of production. Protein L (PpL), isolated from Peptostreptococcus magnus strains, interacts with the Fab (antigen-binding fragment) portion of Igs, specifically with kappa light chains, and represents an almost universal ligand for the purification of antibodies. The concepts of rational design and solid-phase combinatorial chemistry were used for the discovery of a synthetic PpL mimic affinity ligand. The procedure presented in this chapter represents a general approach with the potential to be applied to different systems and target proteins.</p>
},
	url = {http://www.springerprotocols.com/Abstract/doi/10.1007/978-1-59745-582-4_7},
	author = {Roque, A. C. A. and Lowe, C. R.},
	editor = {M. Zachariou}
}
