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| Content Provider | Springer Nature Link |
|---|---|
| Author | Tan, Haidong Dan, Guoping Gong, Huiying Cao, Lijun |
| Copyright Year | 2005 |
| Abstract | 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. |
| Starting Page | 905 |
| Ending Page | 910 |
| Page Count | 6 |
| File Format | |
| ISSN | 01415492 |
| Journal | Biotechnology Letters |
| Volume Number | 27 |
| Issue Number | 13 |
| e-ISSN | 15736776 |
| Language | English |
| Publisher | Kluwer Academic Publishers |
| Publisher Date | 2005-01-01 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | affinity chromatography GST-fusion protein human interleukin-11 Biotechnology Applied Microbiology Biochemistry Microbiology Bioorganic Chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology |
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