Efficient fabrication of high-capacity immobilized metal ion affinity chromatographic media: The role of the dextran-grafting process and its manipulation
文献类型:期刊论文
作者 | Zhao, Lan1; Zhang, Jingfei1,2; Huang, Yongdong1; Li, Qiang1; Zhang, Rongyue3; Zhu, Kai1,4; Suo, Jia3; Su, Zhiguo1; Zhang, Zhigang2; Ma, Guanghui1 |
刊名 | JOURNAL OF SEPARATION SCIENCE
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出版日期 | 2016-03-01 |
卷号 | 39期号:6页码:1130-1136 |
关键词 | Dextran Immobilized metal ion affinity chromatography Nickel Protein purification |
ISSN号 | 1615-9306 |
英文摘要 | Novel high-capacity Ni2+ immobilized metal ion affinity chromatographic media were prepared through the dextran-grafting process. Dextran was grafted to an allyl-activated agarose-based matrix followed by functionalization for the immobilized metal ion affinity chromatographic media. With elaborate regulation of the allylation degree, dextran was completely or partly grafted to agarose microspheres, namely, completely dextran-grafted agarose microspheres and partly dextran-grafted ones, respectively. Confocal laser scanning microscope results demonstrated that a good adjustment of dextran-grafting degree was achieved, and dextran was distributed uniformly in whole completely dextran-grafted microspheres, while just distributed around the outside of the partly dextran-grafted ones. Flow hydrodynamic properties were improved greatly after the dextran-grafting process, and the flow velocity increased by about 30% compared with that of a commercial chromatographic medium (Ni Sepharose FF). A significant improvement of protein binding performance was also achieved by the dextran-grafting process, and partly dextran-grafted Ni2+ chelating medium had a maximum binding capacity for His-tagged lactate dehydrogenase about 2.5 times higher than that of Ni Sepharose FF. The results indicated that this novel chromatographic medium is promising for applications in high-efficiency and large-scale protein purification. |
WOS标题词 | Science & Technology ; Physical Sciences |
类目[WOS] | Chemistry, Analytical |
研究领域[WOS] | Chemistry |
关键词[WOS] | EXCHANGE CHROMATOGRAPHY ; IMMUNOGLOBULIN-G ; AGAROSE MEDIA ; PURIFICATION ; ADSORPTION ; PROTEINS ; ADSORBENT ; RESINS ; TAGS ; GELS |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000373617100013 |
源URL | [http://ir.ipe.ac.cn/handle/122111/20991] ![]() |
专题 | 过程工程研究所_生化工程国家重点实验室 |
作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China 2.Hebei Normal Univ Sci & Technol, Qinhuangdao, Hebei, Peoples R China 3.Beijing Inst Petrochem Technol, Dept Chem Engn, Beijing, Peoples R China 4.China Univ Min & Technol, Sch Chem & Environm Engn, Beijing, Peoples R China |
推荐引用方式 GB/T 7714 | Zhao, Lan,Zhang, Jingfei,Huang, Yongdong,et al. Efficient fabrication of high-capacity immobilized metal ion affinity chromatographic media: The role of the dextran-grafting process and its manipulation[J]. JOURNAL OF SEPARATION SCIENCE,2016,39(6):1130-1136. |
APA | Zhao, Lan.,Zhang, Jingfei.,Huang, Yongdong.,Li, Qiang.,Zhang, Rongyue.,...&Ma, Guanghui.(2016).Efficient fabrication of high-capacity immobilized metal ion affinity chromatographic media: The role of the dextran-grafting process and its manipulation.JOURNAL OF SEPARATION SCIENCE,39(6),1130-1136. |
MLA | Zhao, Lan,et al."Efficient fabrication of high-capacity immobilized metal ion affinity chromatographic media: The role of the dextran-grafting process and its manipulation".JOURNAL OF SEPARATION SCIENCE 39.6(2016):1130-1136. |
入库方式: OAI收割
来源:过程工程研究所
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