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The National Agricultural Library is one of four national libraries of the United States, with locations in Beltsville, Maryland and Washington, D.C. It houses one of the world's largest and most accessible agricultural information collections and serves as the nexus for a national network of state land-grant and U.S. Department of Agriculture field libraries. In fiscal year 2011 (Oct 2010 through Sept 2011) NAL delivered more than 100 million direct customer service transactions.

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Journal Article

Article de revue

Facilitated oxidative refolding of ribonuclease A from inclusion bodies with a new redox system  [2012]

Han, Guang-Jie; Dong, Xiao-Yan; Zhang, Lin; Fu, Li-Tang; et al.

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Oxidative refolding is a crucial step in the bioseparation process of bioactive RNase A from inclusion bodies (IBs) overexpressed in Escherichia coli, and it has been well recognized that RNase A refolding suffers from the slow formation of correct disulfide bonds with traditional redox agents such as reduced glutathione (GSH) and oxidized glutathione (GSSG). Hence, there is demand of developing new redox systems that can accelerate the oxidative refolding of this protein. In this work, a new redox system composed of 4-mercaptobenzeneacetate (ArSH) and hexanoyl cystamine (HCA) was proposed. It was found that the oxidative refolding of RNase A reached a refolding yield of 94% in 2h with ArSH/HCA at optimized concentrations, which was two times faster than that with GSH/GSSG. Moreover, the refolding yield of RNase A from IBs could also reach 89% in 3h with ArSH/HCA, much better than the performance with GSH/GSSG, which was only 69% in 8h refolding. Therefore, the use of the new redox system led to a significant increase of refolding yield and over 60% reduction in the refolding time in the inclusion body protein refolding. The results indicated that the new redox system was much more efficient in the oxidative refolding of RNase A than the traditional redox system.
(Revue
Biochemical engineering journal
ISSN : 1369-703X

Information bibliographique

Langue:
English
Type:
Journal Article
Sur AGRIS depuis:
2016
Volume:
69
Page initiale:
106
Page finale:
112
Editeur:
Elsevier B.V.
Tous les titres:
"Facilitated oxidative refolding of ribonuclease A from inclusion bodies with a new redox system"@eng
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Information bibliographique

Langue:
English
Type:
Journal Article
Sur AGRIS depuis:
2016
Volume:
69
Page initiale:
106
Page finale:
112
Editeur:
Elsevier B.V.
Tous les titres:
"Facilitated oxidative refolding of ribonuclease A from inclusion bodies with a new redox system"@eng