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  • Title: On-column refolding and purification of recombinant human interleukin-1 receptor antagonist (rHuIL-1ra) expressed as inclusion body in Escherichia coli.
    Author: Tan H, Dan G, Gong H, Cao L.
    Journal: Biotechnol Lett; 2005 Aug; 27(16):1177-82. PubMed ID: 16158260.
    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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