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Current Pharmaceutical Biotechnology

Editor-in-Chief

ISSN (Print): 1389-2010
ISSN (Online): 1873-4316

Stress-Free Chromatography: Affinity Chromatography

Author(s): Tsutomu Arakawa, Yoshiko Kita, Haruna Sato and Daisuke Ejima

Volume 10, Issue 4, 2009

Page: [456 - 460] Pages: 5

DOI: 10.2174/138920109788488969

Price: $65

Abstract

A number of approaches are available in minimizing aggregation of the final protein products. This chapter describes one such approach, i.e., an attempt to avoid stressful conditions that may eventually lead to protein aggregation. Affinity chromatography uses specific interaction between protein to be purified and ligand attached to the column. Due to high affinity, dissociation of such interaction and hence elution often require harsh solvent conditions. Ion exchange and hydrophobic interaction chromatography also pose certain stressful conditions on proteins. Here we describe development of mild elution buffer using arginine. This chapter covers Protein-A, dye, Protein-A mimetic and antigen affinity chromatography.


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