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Abstract To obtain Insulin-like growth factor (IGF-1) with high purity and activity; Methods: His-tag-beta-galactosidase-IGF-1 fusion protein was expressed in Escherichia coli as inclusion body with IPTG induction. Cells were then harvested, sonicated and centrifuged , and the inclusion bodies were isolated and purified by Ni2+-high performance affinity chromatography. After cleavage of the fusion protein with hydroxylamine, the released IGF-1 was purified by Ni2+- high performance affinity chromatography again and refolded in the presence of GSH/GSSH. Results: The purity of the released IGF-1 was more than 90% after Ni2+-high performance affinity chromatography, and the refolded IGF-1 was with high biological activities. Conclusion: The procudure of fermentation, simple purification and renaturation of recombinant IGF-1 could build the foundation for the large-scale production of IGF-1.
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Received: 08 September 2005
Published: 25 February 2006
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