A novel protein refolding method integrating ion exchange chromatography with artificial molecular chaperone |
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Authors: | Qin Ming Zhang Chao Zhan Wang Jiang Feng Liu Li Li Wang |
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Affiliation: | Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Institute of Modern Separation Science, Key Laboratory of Separation Science in Shanxi Province, Department of Chemistry, Northwest University, Xi'an 710069, China |
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Abstract: | Artificial molecular chaperone (AMC) and ion exchange chromatography (IEC) were integrated, thus a new refolding method,artificial molecular chaperone-ion exchange chromatography (AMC-IEC) was developed. Compared with AMC and IEC, theactivity recovery of lysozyme obtained by AMC-IEC was much higher in the investigated range of initial protein concentrations,and the results show that AMC-IEC is very efficient for protein refolding at high concentrations. When the initial concentration oflysozyme is 180 mg/mL, its activity recovery obtained by AMC-IEC is still as high as 76.6%, while the activity recoveries obtainedby AMC and IEC are 45.6% and 42.4%, respectively.2008 Chao Zhan Wang. Published by Elsevier B.V. on behalf of Chinese Chemical Society. All rights reserved. |
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Keywords: | Artificial molecular chaperone Ion exchange chromatography Protein refolding Lysozyme Protein folding liquid chromatography |
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