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J Sep Sci. 2017 Apr;40(7):1493-1499. doi: 10.1002/jssc.201601196. Epub 2017 Mar 15.

Enhanced binding by dextran-grafting to Protein A affinity chromatographic media.

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State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, P.R. China.
School of Chemical and Environmental Engineering, China University of Mining and Technology, Beijing, P.R. China.
Department of Chemical Engineering, Beijing Institute of Petro-chemical Technology, Beijing, P.R. China.
Jiangsu National Synergetic Innovation, Center for Advance Materials (SICAM), Nanjing, P.R. China.


Dextran-grafted Protein A affinity chromatographic medium was prepared by grafting dextran to agarose-based matrix, followed by epoxy-activation and Protein A coupling site-directed to sulfhydryl groups of cysteine molecules. An enhancement of both the binding performance and the stability was achieved for this dextran-grafted Protein A chromatographic medium. Its dynamic binding capacity was 61 mg immunoglobulin G/mL suction-dried gel, increased by 24% compared with that of the non-grafted medium. The binding capacity of dextran-grafted medium decreased about 7% after 40 cleaning-in-place cycles, much lower than that of the non-grafted medium as decreased about 15%. Confocal laser scanning microscopy results showed that immunoglobulin G was bound to both the outside and the inside of dextran-grafted medium faster than that of non-grafted one. Atomic force microscopy showed that this dextran-grafted Protein A medium had much rougher surface with a vertical coordinate range of ±80 nm, while that of non-grafted one was ±10 nm. Grafted dextran provided a more stereo surface morphology and immunoglobulin G molecules were more easily to be bound. This high-performance dextran-grafted Protein A affinity chromatographic medium has promising applications in large-scale antibody purification.


Protein A; affinity chromatography; antibody purification; dextran; grafting

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