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Comparative Study
. 2003 Oct;25(20):1729-34.
doi: 10.1023/a:1026050627117.

Refolding of a recombinant full-length non-structural (NS3) protein from hepatitis C virus by chromatographic procedures

Ming Li  1 , Anton Poliakov, U Helena Danielson, Zhiguo Su, Jan-Christer Janson
Affiliations
Comparative Study

Refolding of a recombinant full-length non-structural (NS3) protein from hepatitis C virus by chromatographic procedures

Ming Li et al. Biotechnol Lett. 2003 Oct.

Abstract

The non-structural protein 3 (NS3) of Hepatitis C virus (HCV) was expressed as inactive aggregates in Escherichia coli. The protein was refolded by chromatographic techniques of which ion exchange chromatography was best for crude samples and gel filtration best for partially purified samples. Immobilized metal ion affinity chromatography showed intermediate performance. Gradient procedures enhanced the recovery of active NS3 protein.

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