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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 PublicationJOURNAL OF SEPARATION SCIENCE
ISSN1615-9306
Volume40Issue: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.

KeywordAffinity Chromatography Antibody Purification Dextran Grafting Protein a
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
DOI10.1002/jssc.201601196
Indexed BySCI
Language英语
WOS KeywordMixed-mode Chromatography ; Monoclonal-antibody ; Ion-exchange ; Immunoglobulin-g ; Purification ; Adsorption ; Transport ; Manipulation ; Orientation ; Adsorbent
WOS Research AreaChemistry
WOS SubjectChemistry, Analytical
Funding OrganizationNatural 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 IDWOS:000399782900007
Citation statistics
Cited Times:7[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/22825
Collection生化工程国家重点实验室
Affiliation1.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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