Refolding of protein from denatured state to active conformation by liquid chromatographic processes
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Refolding of protein from denatured state to active conformation by liquid chromatographic processes
CIESC JournalIssue 8, Pages: 1802-1809(2006)
作者机构:
1. 中国科学院过程工程研究所生化工程国家重点实验室,北京,100080
2. 中国科学院研究生院,北京,100080
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Online First:25 August 2006,
Published:25 August 2006
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CHEN Jing, LIU Yongdong, LI Jingjing, et al. Refolding of protein from denatured state to active conformation by liquid chromatographic processes[J]. CIESC Journal, 2006, (8): 1802-1809.
DOI:
CHEN Jing, LIU Yongdong, LI Jingjing, et al. Refolding of protein from denatured state to active conformation by liquid chromatographic processes[J]. CIESC Journal, 2006, (8): 1802-1809.DOI:
Refolding of protein from denatured state to active conformation by liquid chromatographic processes
Chromatography is commonly used in separating expensive fine chemical products.Liquid chromatographic procedure is the essential tool in protein purification because of its mild condition
quick and effective separation.In recent years
chromatography has been gradually used in protein refolding from denatured state to biologically active conformation.In the liquid chromatography-based protein refolding procedure
a high yield could be achieved at high protein concentrations.Partial purification of protein could also be achieved simultaneously.The recent development of liquid chromatography-based protein refolding is reviewed in this paper.The principles
advantages
disadvantages and applications are discussed with respect to various chromatographic refolding processes
including size exclusion chromatography
ion exchange chromatography
hydrophobic interaction chromatography
affinity chromatography with immobilized refolding catalyst and artificial chaperone.