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- Title
Improved purification of immunoglobulin G from plasma by mixed-mode chromatography.
- Authors
Chai, Dong‐Sheng; Sun, Yan; Wang, Xiao‐Ning; Shi, Qing‐Hong
- Abstract
Efficient loading of immunoglobulin G in mixed-mode chromatography is often a serious bottleneck in the chromatographic purification of immunoglobulin G. In this work, a mixed-mode ligand, 4-(1 H-imidazol-1-yl) aniline, was coupled to Sepharose Fast Flow to fabricate AN SepFF adsorbents with ligand densities of 15-64 mmol/L, and the chromatographic performances of these adsorbents were thoroughly investigated to identify a feasible approach to improve immunoglobulin G purification. The results indicate that a critical ligand density exists for immunoglobulin G on the AN SepFF adsorbents. Above the critical ligand density, the adsorbents showed superior selectivity to immunoglobulin G at high salt concentrations, and also exhibited much higher dynamic binding capacities. For immunoglobulin G purification, both the yield and binding capacity increased with adsorbent ligand density along with a decrease in purity. It is difficult to improve the binding capacity, purity, and yield of immunoglobulin G simultaneously in AN SepFF chromatography. By using tandem AN SepFF chromatography, a threefold increase in binding capacity as well as high purity and yield of immunoglobulin G were achieved. Therefore, the tandem chromatography demonstrates that AN SepFF adsorbent is a practical and feasible alternative to MEP HyperCel adsorbents for immunoglobulin G purification.
- Subjects
IMMUNOGLOBULIN G; LIQUID chromatography; LIGANDS (Biochemistry); IMIDAZOLES; BINDING sites
- Publication
Journal of Separation Science, 2014, Vol 37, Issue 23, p3461
- ISSN
1615-9306
- Publication type
Article
- DOI
10.1002/jssc.201400554