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Updated: Aug 15, 2026

Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
Selective non-adsorption preparative chromatography of bovine immunoglobulin Gl
1Department of Biochemistry, Purdue University, West Lafayette, IN 47907.
Abstract:
Bovine immunoglobulin Gl (IgGl) was purified from blood serum by isocratic elution through a mixed-bed ion-exchange column at low ionic strength. Selection of a mobile phase pH near the isoelectric point of IgG precluded its binding to the strong cation- and anion-exchange sorbents and allowed IgGl to be eluted isocratically. Under these conditions most of the other components in the serum sample were retained on the mixed-bed column. This approach gives excellent throughput and purity.
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