A newly proposed mechanism for arginine-assisted protein refolding - not inhibiting soluble oligomers although promoting a correct structure
文献类型：期刊论文
| 作者 | Liu, Yong-dong; Li, Jing-jing; Wang, Fang-wei; Chen, Jing; Li, Peng; Su, Zhi-guo |
| 刊名 | PROTEIN EXPRESSION AND PURIFICATION
 |
| 出版日期 | 2007-02-01 |
| 卷号 | 51期号:2页码:235-242 |
| 关键词 | refolding additives arginine recombinant consensus interferon |
| ISSN号 | 1046-5928 |
| 其他题名 | Protein Expr. Purif. |
| 中文摘要 | Arginine has been demonstrated to be capable of suppressing aggregation during protein refolding. However, the pathway and the mechanism for arginine to participate in and to assist refolding process still remains unclear. In this study, arginine-assisted refolding of recombinant consensus interferon (rIFN-con(1)) was investigated. It was found that although arginine minimized the formation of protein precipitate, it failed to prevent the formation of the soluble oligomeric species. The amount of the oligomers increased with the increase in arginine concentration. This phenomenon has not been reported. On the other hand, arginine was able to promote the yield of correctly refolded rIFN-con(1), which was more than 2 times higher than that in the absence of arginine. A proposed mechanism is the stabilization of different soluble species by arginine, which slowed down the conformational movement. The stabilization effect on native-like structure formation overwhelmed the oligomeric promotion effect, which resulted in a composite effect of increased refolding yield for rIFN-con, when arginine concentration was below 0.5 M. (c) 2006 Elsevier Inc. All rights reserved. |
| 英文摘要 | Arginine has been demonstrated to be capable of suppressing aggregation during protein refolding. However, the pathway and the mechanism for arginine to participate in and to assist refolding process still remains unclear. In this study, arginine-assisted refolding of recombinant consensus interferon (rIFN-con(1)) was investigated. It was found that although arginine minimized the formation of protein precipitate, it failed to prevent the formation of the soluble oligomeric species. The amount of the oligomers increased with the increase in arginine concentration. This phenomenon has not been reported. On the other hand, arginine was able to promote the yield of correctly refolded rIFN-con(1), which was more than 2 times higher than that in the absence of arginine. A proposed mechanism is the stabilization of different soluble species by arginine, which slowed down the conformational movement. The stabilization effect on native-like structure formation overwhelmed the oligomeric promotion effect, which resulted in a composite effect of increased refolding yield for rIFN-con, when arginine concentration was below 0.5 M. (c) 2006 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] | EGG-WHITE LYSOZYME ; INCLUSION-BODIES ; OXIDATIVE RENATURATION ; AGGREGATION ; INTERFERON ; SOLUBILIZATION ; STABILIZATION ; PURIFICATION ; YIELD |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000244210100013 |
| 公开日期 | 2013-10-15 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/3397]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100080, Peoples R China 2.Dalian Univ Technol, Dalian 116024, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Yong-dong,Li, Jing-jing,Wang, Fang-wei,et al. A newly proposed mechanism for arginine-assisted protein refolding - not inhibiting soluble oligomers although promoting a correct structure[J]. PROTEIN EXPRESSION AND PURIFICATION,2007,51(2):235-242. |
| APA | Liu, Yong-dong,Li, Jing-jing,Wang, Fang-wei,Chen, Jing,Li, Peng,&Su, Zhi-guo.(2007).A newly proposed mechanism for arginine-assisted protein refolding - not inhibiting soluble oligomers although promoting a correct structure.PROTEIN EXPRESSION AND PURIFICATION,51(2),235-242. |
| MLA | Liu, Yong-dong,et al."A newly proposed mechanism for arginine-assisted protein refolding - not inhibiting soluble oligomers although promoting a correct structure".PROTEIN EXPRESSION AND PURIFICATION 51.2(2007):235-242. |
入库方式： OAI收割
来源：过程工程研究所
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