Protein A chromatography for antibody purification

  • J Chromatogr B Analyt Technol Biomed Life Sci. 2007 Mar 15;848(1):40-7. doi: 10.1016/j.jchromb.2006.09.030.
Sophia Hober  1 ,  Karin Nord ,  Martin Linhult
Affiliations
  • 1. Royal Institute of Technology, Stockholm, Sweden.
PMID: 17030158 DOI: 10.1016/j.jchromb.2006.09.030
Abstract

Staphylococcal protein A (SPA) is one of the first discovered immunoglobulin binding molecules and has been extensively studied during the past decades. Due to its affinity to immunoglobulins, SPA has found widespread use as a tool in the detection and purification of antibodies and the molecule has been further developed to one of the most employed affinity purification systems. Interestingly, a minimized SPA derivative has been constructed and a domain originating from SPA has been improved to withstand the harsh environment employed in industrial purifications. This review will focus on the development of different affinity molecules and matrices for usage in antibody purification.