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

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons86356

Keßler,  L. C.
Physical and Chemical Foundations of Process Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons86477

Seidel-Morgenstern,  A.
Physical and Chemical Foundations of Process Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society;
Otto-von-Guericke-Universität Magdeburg, External Organizations;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0013-997F-6
Abstract
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.