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Cooperative effects of urea and L-arginine on protein refolding
Chen, Jing1,2; Liu, Yongdong1; Li, Xiunan1; Wang, Yinjue1,2; Ding, Hong1; Ma, Guanghui1; Su, Zhiguo1; Su, ZG
2009-07-01
Source PublicationPROTEIN EXPRESSION AND PURIFICATION
ISSN1046-5928
Volume66Issue:1Pages:82-90
AbstractThe 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.
KeywordRefolding Kinetics Urea L-arginine Guanidinium Chloride Rhg-csf
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1016/j.pep.2009.02.004
Indexed BySCI
Language英语
WOS KeywordCOLONY-STIMULATING FACTOR ; HYDROPHOBIC INTERACTION ; GUANIDINIUM CHLORIDE ; PROPOSED MECHANISM ; GROWTH-FACTORS ; AGGREGATION ; LYSOZYME ; RENATURATION ; DISULFIDE
WOS Research AreaBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS SubjectBiochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS IDWOS:000265346000013
Citation statistics
Cited Times:36[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/6644
Collection生化工程国家重点实验室
Corresponding AuthorSu, ZG
Affiliation1.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
Recommended Citation
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, ZG.(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.
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