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  Purification of Immunoglobulin G using different matrices in simulated moving bed chromatography

Keßler, L. C., & Seidel-Morgenstern, A. (2006). Purification of Immunoglobulin G using different matrices in simulated moving bed chromatography. Poster presented at ISPPP 2006: 26th International Symposium on the Separation of Proteins, Peptides and Polynucleotides, Innsbruck, Austria.

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 Urheber:
Keßler, L. C.1, Autor           
Seidel-Morgenstern, A.1, 2, Autor           
Affiliations:
1Physical and Chemical Foundations of Process Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society, ou_1738150              
2Otto-von-Guericke-Universität Magdeburg, External Organizations, ou_1738156              

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 Zusammenfassung: In the course of the last decade the interest in therapeutic monoclonal antibodies has increased continuously. Consequently an effective purification scheme is of great interest. In most cases protein A affinity chromatography is used. However, due to the high costs of the stationary phases and the potential leakage of ligands there is a trend towards other modes of operation [1]. Simulated moving bed chromatography (SMB) has been considered as an interesting alternative [2]; applications however are still far from common. In this work we present the separation of bovine Immunoglobulin G (IgG) from three model mixtures. Differently functionalised resins for ion-exchange, hydrophobic interaction and size-exclusion chromatography were investigated systematically regarding their adsorption and retention properties for IgG. The obtained parameters were used to calculate appropriate operating conditions for the separation in SMB chromatography.

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Sprache(n): eng - English
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 Identifikatoren: eDoc: 283478
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Titel: ISPPP 2006 : 26th International Symposium on the Separation of Proteins, Peptides and Polynucleotides
Veranstaltungsort: Innsbruck, Austria
Start-/Enddatum: 2006-10-18 - 2006-10-20

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