Abstract
Recent developments in recombinant DNA technology have enabled the synthesis of valuable therapeutic proteins in bacterial cells as well as in novel eucaryotic expression systems. However, the purification of proteins of interest from either the conventional sources, cell culture, or novel routes in a highly purified form necessitates the development of separation techniques capable of recovering proteins from these feed streams in a highly purified form (1,2). Purification of therapeutic proteins from biological sources is usually complicated by the presence of endogenous proteins (2). Purification methodologies based on ion exchange or adsorption serve as excellent prepurification steps, but they fail to resolve complex protein mixtures to yield a homogeneous protein product (1). Purification techniques based on affinity interactions between molecules (i.e., immunoaffinity chromatography, IAC) have rapidly evolved using a variety of biological and synthetic ligands (2).
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Subramanian, A. (2000). Immunoaffinity Chromatography. In: Bailon, P., Ehrlich, G.K., Fung, WJ., Berthold, W. (eds) Affinity Chromatography. Methods in Molecular Biology, vol 147. Humana Press. https://doi.org/10.1007/978-1-60327-261-2_10
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DOI: https://doi.org/10.1007/978-1-60327-261-2_10
Publisher Name: Humana Press
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Online ISBN: 978-1-60327-261-2
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