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

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.