DICP OpenIR
Purification and characterization of recombinant truncated human interleukin-11 expressed as fusion protein in Escherichia coli
Tan, HD; Dan, GP; Gong, HY; Cao, LJ; Tan HD(谭海东); Tan HD(谭海东)
KeywordAffinity Chromatography Gst-fusion Protein Human Interleukin-11
Source PublicationBIOTECHNOLOGY LETTERS
2005-07-01
ISSN0141-5492 (Paper) 1573-6776 (Online)
DOI10.1007/s10529-005-7179-3
Volume27Issue:13Pages:905-910
Indexed BySCI
SubtypeArticle
Department18
Funding Project1816
Contribution Rank1;1
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiotechnology & Applied Microbiology
WOS Research AreaBiotechnology & Applied Microbiology
WOS KeywordRHEUMATOID-ARTHRITIS ; INTERLEUKIN-11 ; CELLS
AbstractMature 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.
Language英语
URL查看原文
WOS IDWOS:000231164000004
Citation statistics
Cited Times:10[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/93187
Collection中国科学院大连化学物理研究所
Corresponding AuthorTan HD(谭海东); Tan HD(谭海东)
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
2.Duotai Biopharmaceut Co Ltd, Chongqing 200400, Peoples R China
Recommended Citation
GB/T 7714
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.
APA Tan, HD,Dan, GP,Gong, HY,Cao, LJ,谭海东,&谭海东.(2005).Purification and characterization of recombinant truncated human interleukin-11 expressed as fusion protein in Escherichia coli.BIOTECHNOLOGY LETTERS,27(13),905-910.
MLA Tan, HD,et al."Purification and characterization of recombinant truncated human interleukin-11 expressed as fusion protein in Escherichia coli".BIOTECHNOLOGY LETTERS 27.13(2005):905-910.
Files in This Item:
File Name/Size DocType Version Access License
2005830W2N9BQT.pdf(276KB) 开放获取--Application Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Tan, HD]'s Articles
[Dan, GP]'s Articles
[Gong, HY]'s Articles
Baidu academic
Similar articles in Baidu academic
[Tan, HD]'s Articles
[Dan, GP]'s Articles
[Gong, HY]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Tan, HD]'s Articles
[Dan, GP]'s Articles
[Gong, HY]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.