Cooperative effects of urea and L-arginine on protein refolding
文献类型：期刊论文
| 作者 | Chen, Jing1,2; Liu, Yongdong1; Li, Xiunan1; Wang, Yinjue1,2; Ding, Hong1; Ma, Guanghui1; Su, Zhiguo1 |
| 刊名 | PROTEIN EXPRESSION AND PURIFICATION
 |
| 出版日期 | 2009-07-01 |
| 卷号 | 66期号:1页码:82-90 |
| 关键词 | Refolding kinetics Urea L-Arginine Guanidinium chloride rhG-CSF |
| ISSN号 | 1046-5928 |
| 通讯作者 | Su, ZG |
| 英文摘要 | The use of low concentrations of urea, guanidinium chloride or arginine has been reported in the literature to increase protein refolding and yield of active proteins by suppressing aggregate formation. However, no studies have yet examined whether these substances can exert synergistic or cooperative effects when used in combination. In this work, a comparative study was carried out on refolding of recombinant human granulocyte colony-stimulating factor (rhG-CSF) in the presence of different concentrations of urea, guanidinium chloride or arginine. All three folding aids could inhibit the formation of insoluble aggregates of rhG-CSF but with different efficacies. A low concentration of guanidinium chloride was found to denature protein, so that rhG-CSF was not fully or correctly folded even if concentration was reduced to I M. Low concentration of urea (2 M) or arginine (0.5 M) did not cause rhG-CSF denaturation, but urea was unable to suppress the formation of soluble oligomers, which persisted at a level of about 30% in refolded soluble rhG-CSF. Arginine, in contrast, could inhibit formation of all soluble oligomers. Based on these phenomena, we tested rhG-CSF folding in a mixture of 2 M urea and 0.5 M arginine. Kinetic analysis indicated that urea aided in suppressing insoluble precipitates, while arginine prevented formation of soluble oligomers produced by hydrophobic interaction. With this combination system, the refolding yield of rhG-CSF could be increased 2-fold. (C) 2009 Elsevier Inc. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 关键词[WOS] | COLONY-STIMULATING FACTOR ; HYDROPHOBIC INTERACTION ; GUANIDINIUM CHLORIDE ; PROPOSED MECHANISM ; GROWTH-FACTORS ; AGGREGATION ; LYSOZYME ; RENATURATION ; DISULFIDE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000265346000013 |
| 公开日期 | 2013-12-06 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/6644]  |
| 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.Chinese Acad Sci, Grad Sch, Beijing 100190, Peoples R China |
| 推荐引用方式 GB/T 7714 | Chen, Jing,Liu, Yongdong,Li, Xiunan,et al. Cooperative effects of urea and L-arginine on protein refolding[J]. PROTEIN EXPRESSION AND PURIFICATION,2009,66(1):82-90. |
| APA | Chen, Jing.,Liu, Yongdong.,Li, Xiunan.,Wang, Yinjue.,Ding, Hong.,...&Su, Zhiguo.(2009).Cooperative effects of urea and L-arginine on protein refolding.PROTEIN EXPRESSION AND PURIFICATION,66(1),82-90. |
| MLA | Chen, Jing,et al."Cooperative effects of urea and L-arginine on protein refolding".PROTEIN EXPRESSION AND PURIFICATION 66.1(2009):82-90. |
入库方式： OAI收割
来源：过程工程研究所
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