Enhanced binding by dextran-grafting to Protein A affinity chromatographic media | |
Zhao, Lan1; Zhu, Kai1,2; Huang, Yongdong1; Li, Qiang1; Li, Xiunan1; Zhang, Rongyue3; Su, Zhiguo1; Wang, Qibao2; Ma, Guanghui1,4 | |
2017-04-01 | |
Source Publication | JOURNAL OF SEPARATION SCIENCE
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ISSN | 1615-9306 |
Volume | 40Issue:7Pages:1493-1499 |
Abstract | 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. |
Keyword | Affinity Chromatography Antibody Purification Dextran Grafting Protein a |
Subtype | Article |
WOS Headings | Science & Technology ; Physical Sciences |
DOI | 10.1002/jssc.201601196 |
Indexed By | SCI |
Language | 英语 |
WOS Keyword | Mixed-mode Chromatography ; Monoclonal-antibody ; Ion-exchange ; Immunoglobulin-g ; Purification ; Adsorption ; Transport ; Manipulation ; Orientation ; Adsorbent |
WOS Research Area | Chemistry |
WOS Subject | Chemistry, Analytical |
Funding Organization | Natural Sciences Foundation of China(21306206 ; National Key Technology R&D Program of the Ministry of Science and Technology(2013BAB01B03) ; National High Technology Research and Development Program of China (863 Program)(2014AA021006) ; National Key Scientific Instrument and Equipment Development Project(2013YQ14040502) ; National Key Research and Development Program of China(2016YFF0202304) ; Beijing Natural Science Foundation(2172054) ; 21206175 ; 21476241) |
WOS ID | WOS:000399782900007 |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | http://ir.ipe.ac.cn/handle/122111/22825 |
Collection | 生化工程国家重点实验室 |
Affiliation | 1.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing, Peoples R China 2.China Univ Min & Technol, Sch Chem & Environm Engn, Beijing, Peoples R China 3.Beijing Inst Petrochem Technol, Dept Chem Engn, Beijing, Peoples R China 4.Ctr Adv Mat SICAM, Jiangsu Natl Synerget Innovat, Nanjing, Jiangsu, Peoples R China |
Recommended Citation GB/T 7714 | Zhao, Lan,Zhu, Kai,Huang, Yongdong,et al. Enhanced binding by dextran-grafting to Protein A affinity chromatographic media[J]. JOURNAL OF SEPARATION SCIENCE,2017,40(7):1493-1499. |
APA | Zhao, Lan.,Zhu, Kai.,Huang, Yongdong.,Li, Qiang.,Li, Xiunan.,...&Ma, Guanghui.(2017).Enhanced binding by dextran-grafting to Protein A affinity chromatographic media.JOURNAL OF SEPARATION SCIENCE,40(7),1493-1499. |
MLA | Zhao, Lan,et al."Enhanced binding by dextran-grafting to Protein A affinity chromatographic media".JOURNAL OF SEPARATION SCIENCE 40.7(2017):1493-1499. |
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