| Refolding of urea-denatured α-chymotrypsin by protein-folding liquid chromatography. | |
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MedLine Citation:
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PMID: 23033217 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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An approach for re-folding denatured proteins during proteome research by protein folding liquid chromatography (PFLC) is presented. Standard protein, α-chymotrypsin (α-Chy), was selected as a model protein and hydrophobic interaction chromatography was performed as a typical PFLC; the three different α-Chy states - urea-denatured (U state), its folded intermediates (M state) and nature state (N state) - were studied during protein folding. Based on the test by matrix-assisted laser desorption/ionization time of flight mass spectrometry and bioactivity, only one stable M state of the α-Chy was identified and then it was prepared for further investigation. The specific bioactivity of the refolded α-Chy was found to be higher than that of commercial α-Chy as the urea concentration in the sample solution ranged from 1.0 to 3.0 m; the highest specific bioactivity at urea concentration was 1.0 m, indicating the possibility for re-folding some proteins that have partially or completely lost their bioactivity, as a dilute urea solution was employed for dissolving the sample. The experiment showed that the peak height of its M state increased with increasing urea concentration, and correspondingly decreased in the amount of the refolded α-Chy. When the urea concentration reached 6.0 m, the unfolded α-Chy could not be refolded at all. Copyright © 2012 John Wiley & Sons, Ltd. |
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Authors:
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Ke Congyu; Sun Wujuan; Zhang Qunzheng; Geng Xindu |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-10-3 |
Journal Detail:
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Title: Biomedical chromatography : BMC Volume: - ISSN: 1099-0801 ISO Abbreviation: Biomed. Chromatogr. Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-3 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8610241 Medline TA: Biomed Chromatogr Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2012 John Wiley & Sons, Ltd. |
Affiliation:
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College of Chemistry & Chemical Engineering, Xi' An ShiYou University, Xi'an, 710065, China. kcy@xsyu.edu.cn. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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