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Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
Antibody purification from human plasma by metal-chelated affinity membranes
Handan Yavuz1, Nilay Bereli, Fatma Yılmaz
1Biochemistry Division, Department of Chemistry, Hacettepe University, Chemistry Department, Ankara, 06800, Turkey.
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, Zn(2+), Ni(2+), Co(2+), and Cu(2+) ions were chelated directly on the poly(HEMA-MAH) membranes for purification of immunoglobulin G (IgG) from human plasma.
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