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题名: Purification and characterization of recombinant truncated human interleukin-11 expressed as fusion protein in Escherichia coli
作者: Tan, HD;  Dan, GP;  Gong, HY;  Cao, LJ
通讯作者: 谭海东
关键词: affinity chromatography ;  GST-fusion protein ;  human interleukin-11
刊名: BIOTECHNOLOGY LETTERS
发表日期: 2005-07-01
DOI: 10.1007/s10529-005-7179-3
卷: 27, 期:13, 页:905-910
收录类别: SCI
文章类型: Article
部门归属: 18
项目归属: 1816
产权排名: 1;1
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biotechnology & Applied Microbiology
研究领域[WOS]: Biotechnology & Applied Microbiology
英文摘要: Mature human interleukin-11 (HuIL-11) is a cytokine consisting of 178 amino acid residues that results from scission of the N-terminal signal peptide, consisting of 21 amino acid residaues, from the corresponding nascent polypeptide. A DNA fragment encoding a truncated HuIL-11 (trHuIL-11), with an additional 5 amino acid residues removed from the N-terminus, was cloned into vector pGEX-2T between the BamHI site and the EcoRI site. Upon transformation with Escherichia coli BL21, the construct over-produced a glutathione S-transferase (GST)-fused protein in a soluble form after IPTG induction. The fusion protein was initially fractionated with butyl-Sepharose 4 fast flow column and by affinity chromatography using a GSH-Sepharose 4B column. On-site enzymatic release with thrombin gave the target protein at 96% purity as judged by SDS-PAGE and HPLC. Expression of the interleukin as a GST-fused protein thus greatly improved downstream processing. Subsequent biological activity assay suggested that trHuIL-11 had similar activity profile to the naturally produced sample and may be a promising candidate for further development as biopharmaceutical.
关键词[WOS]: RHEUMATOID-ARTHRITIS ;  INTERLEUKIN-11 ;  CELLS
语种: 英语
原文出处: 查看原文
WOS记录号: WOS:000231164000004
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/93187
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
2.Duotai Biopharmaceut Co Ltd, Chongqing 200400, Peoples R China

Recommended Citation:
Tan, HD,Dan, GP,Gong, HY,et al. Purification and characterization of recombinant truncated human interleukin-11 expressed as fusion protein in Escherichia coli[J]. BIOTECHNOLOGY LETTERS,2005,27(13):905-910.
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