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On-Column Refolding and Purification of Recombinant Human Interleukin-1 Receptor Antagonist (rHuIL-1ra) Expressed as Inclusion Body in Escherichia coli

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An Erratum to this article was published on 06 February 2007

Abstract

Recombinant human interleukin-1 receptor antagonist (rHuIL-1ra) was produced in E. coli as an inclusion body. rHuIL-1ra was purified to Over 98% purity by anion exchange chromatography after on-column refolding. The optimized processes produced more than 2 g pure refolded rHuIL-1ra per 1 l culture, corresponding to a 44% recovery, without an intermediate dialysis step. Refolded rHuIL-1ra had full biological activity with the MTT assay. An intramolecular disulfide linkage in the oxidized recombinant protein was suggested by data from HPLC and non-reducing SDS-PAGE.

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Correspondence to Haidong Tan.

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An erratum to this article is available at http://dx.doi.org/10.1007/s10529-006-9306-1.

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Tan, H., Dan, G., Gong, H. et al. On-Column Refolding and Purification of Recombinant Human Interleukin-1 Receptor Antagonist (rHuIL-1ra) Expressed as Inclusion Body in Escherichia coli . Biotechnol Lett 27, 1177–1182 (2005). https://doi.org/10.1007/s10529-005-8655-5

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  • DOI: https://doi.org/10.1007/s10529-005-8655-5

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