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A mild hydrophobic interaction chromatography involving polyethylene glycol immobilized to agarose media refolding recombinant Staphylococcus aureus elongation factor G
Li, JJ; Venkataramana, M; Wang, AQ; Sanyal, S; Janson, JC; Su, ZG
2005-04-01
Source PublicationPROTEIN EXPRESSION AND PURIFICATION
ISSN1046-5928
Volume40Issue:2Pages:327-335
AbstractRecombinant Staphylococcus aureus elongation factor G (EF-G) is difficult to refold by dilution due to the formation of large amounts of misfolded structures. However, refolding of EF-G by adsorption to a chromatographic column packed with immobilized polyethylene glycol 20,000 (PEG 20 K) followed by pulse elution with 8 M urea resulted in 88% mass recovery and 80% of correctly refolded structure. The PEG 20 K was coupled to brominated allyl group derivatized Sepharose High Performance to construct a mild hydrophobic adsorbent. Various other hydrophobic interaction adsorbents were also attempted to retold EF-G. However, ligands with high hydrophobicity tended to misfold EF-G, resulting in irreversible adsorption. Various solvents, detergents, and low temperature as well as 8 M urea were tried to release bound EF-G. Only pulse elution with 8 M urea was efficient. Urea concentrations favorable for efficiently refolding EF-G were investigated. Low urea concentration produced more misfolded structures. (c) 2005 Elsevier Inc. All rights reserved.
KeywordElongation Factor g Refolding Immobilized Polyethylene Glycol Hydrophobic Interaction Chromatography Pulse Elution Urea
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1016/j.pep.2004.12.029
Indexed BySCI
Language英语
WOS KeywordINCLUSION-BODIES ; FUSIDIC ACID ; LYSOZYME ; AGGREGATION ; PROTEINS
WOS Research AreaBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS SubjectBiochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS IDWOS:000227889600013
Citation statistics
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/1582
Collection生化工程国家重点实验室
Affiliation1.Chinese Acad Sci, Natl Key Lab Biochem Engn, Inst Proc Engn, Beijing 100080, Peoples R China
2.Uppsala Univ, Dept Cell & Mol Biol, BMC, SE-75124 Uppsala, Sweden
3.Uppsala Univ, Dept Surface Biotechnol, BMC, SE-75123 Uppsala, Sweden
Recommended Citation
GB/T 7714
Li, JJ,Venkataramana, M,Wang, AQ,et al. A mild hydrophobic interaction chromatography involving polyethylene glycol immobilized to agarose media refolding recombinant Staphylococcus aureus elongation factor G[J]. PROTEIN EXPRESSION AND PURIFICATION,2005,40(2):327-335.
APA Li, JJ,Venkataramana, M,Wang, AQ,Sanyal, S,Janson, JC,&Su, ZG.(2005).A mild hydrophobic interaction chromatography involving polyethylene glycol immobilized to agarose media refolding recombinant Staphylococcus aureus elongation factor G.PROTEIN EXPRESSION AND PURIFICATION,40(2),327-335.
MLA Li, JJ,et al."A mild hydrophobic interaction chromatography involving polyethylene glycol immobilized to agarose media refolding recombinant Staphylococcus aureus elongation factor G".PROTEIN EXPRESSION AND PURIFICATION 40.2(2005):327-335.
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