Enhanced In vitro refolding selectivity of the recombinant human insulin-like growth factor I

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Title
Enhanced In vitro refolding selectivity of the recombinant human insulin-like growth factor I
Author(s)
Sun-Ok Kim; Young Ik Lee
Bibliographic Citation
Biotechnology Techniques, vol. 11, no. 2, pp. 85-89
Publication Year
1997
Abstract
A systematic study was carried out to optimize production of biologically active recombinant IGF-I with native conformation. Careful optimization of buffer carbonate, pH (9.5), protein concentration (0.5 mg/ml), temperature (25°C), and disulfide-exchange reagents (2 mM reduced glutathione/1 mM oxidized glutathione, 1 mM cysteine, 1 mM β-mercaptoethanol, and 2 mM dithiothreitol) allowed a yield of correctly folded recombinant IGF-I as high as 80%, which may be useful for large scale production of IGF-I.
Keyword
Growth FactorGlutathioneCysteineProtein ConcentrationSystematic Study
ISSN
0951-208X
Publisher
Springer
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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