Abstract
Immobilized metal ion affinity chromatography (IMAC) has been used for purification of proteins. IMAC introduces a new approach for selectively interacting biomolecules on the basis of their affinities for metal ions. The separation is based on different binding abilities of the proteins to the chelated metal ions on support. Here, N-methacryloyl-(l)-histidine methyl ester (MAH) is used as the metal-chelating ligand. Poly(hydroxyethyl methacrylate) Poly(HEMA) based membranes were prepared by photo-polymerization technique. Then, Zn2+, Ni2+, Co2+, and Cu2+ ions were chelated directly on the poly(HEMA-MAH) membranes for purification of immunoglobulin G (IgG) from human plasma.
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Yavuz, H., Bereli, N., Yılmaz, F., Armutcu, C., Denizli, A. (2015). Antibody Purification from Human Plasma by Metal-Chelated Affinity Membranes. In: Reichelt, S. (eds) Affinity Chromatography. Methods in Molecular Biology, vol 1286. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2447-9_4
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DOI: https://doi.org/10.1007/978-1-4939-2447-9_4
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-2446-2
Online ISBN: 978-1-4939-2447-9
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