右旋糖酐
化学
色谱法
嫁接
琼脂糖
琼脂糖
亲和层析
基质(化学分析)
蛋白质A
抗体
生物化学
聚合物
有机化学
酶
生物
免疫学
作者
Lan Zhao,K. J. Zhu,Yongdong Huang,Qiang Li,Xiunan Li,Rongyue Zhang,Zhiguo Su,Qibao Wang,Guanghui Ma
标识
DOI:10.1002/jssc.201601196
摘要
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.
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