On-Column Refolding and Purification of Recombinant Human Interleukin-1 Receptor Antagonist (rHuIL-1ra) Expressed as Inclusion Body in <Emphasis Type="Italic">Escherichia coli</Emphasis>期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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

Authors:	Haidong?Tan author-information" > author-information__contact u-icon-before" > mailto:hdt@dicp.ac.cn" title=" hdt@dicp.ac.cn" itemprop=" email" data-track=" click" data-track-action=" Email author" data-track-label=" " >Email author,Guoping?Dan,Huiying?Gong,Lijun?Cao

Affiliation:	(1) Dalian Institute of Chemical Physics, CAS, 457 Zhongshan Road, 116023, Dalian, P.R. China;(2) Yushui Biopharmaceutical Co., Ltd, 200400, Chongqing, P.R. China

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.

Keywords:	human interleukin-1 receptor antagonist inclusion body on-column refolding
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