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Protein A chromatography for antibody purification
KTH, School of Biotechnology (BIO), Proteomics.ORCID iD: 0000-0003-0605-8417
2007 (English)In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 848, no 1, 40-47 p.Article, review/survey (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2007. Vol. 848, no 1, 40-47 p.
Keyword [en]
affinity chromatography, cleaning-in-place (CIP), deamidation, protein A, protein engineering, stabilization, affinity-chromatography, monoclonal-antibodies, staphylococcus-aureus, synthetic ligand, immunoglobulin-g, phage display, binding, sorbents, deamidation, peptides
URN: urn:nbn:se:kth:diva-16527DOI: 10.1016/j.chromb.2006.09.030ISI: 000245491300006ScopusID: 2-s2.0-33847660116OAI: diva2:334569
QC 20100525Available from: 2010-08-05 Created: 2010-08-05Bibliographically approved

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