Journal
JOURNAL OF CHROMATOGRAPHY A
Volume 1216, Issue 24, Pages 4902-4912Publisher
ELSEVIER
DOI: 10.1016/j.chroma.2009.04.014
Keywords
2-D DIGE; IgG; Recombinant antibody; Staphylococcus Protein A chromatography; Affinity chromatography; Ion exchange chromatography
Funding
- Biomedical Research Council
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Although Staphylococcus Protein A (SpA) affinity chromatography is the state of the art capture step for antibody purification, non-affinity methods are more economical. We used two-dimensional fluorescence difference gel electrophoresis (2-D DIGE) to evaluate the purification Of a recombinant IgG(1) antibody from cultured cells, with two different processes: (I) SpA capture followed by cation-exchange chromatography (CEX); and (2) CEX capture, followed by anion exchanger, then hydrophobic interaction chromatography. Efficiencies were similar in sodium dodecylsulphate polyacrylamide gel electrophoresis and size-exclusion chromatography; however, 2-D DIGE revealed higher efficiency with SpA than with CEX capture. Thus, 2-D DIGE is a Valuable tool for downstream process development. (C) 2009 Elsevier B.V. All rights reserved.
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