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中国生物工程杂志

China Biotechnology
China Biotechnology
    
Site-specific PEGylation of engineered cysteine analogues of recombinant human interleukin-11
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Abstract  

Human Interleukin-11(hIL-11) has no Cys residue in its natural form. By site-directed mutagenesis ,a Cys residue can be introduced to replace the 1st residue Gly and the rhIL11 was chemically modified by using 20 kDa mPEG-maleimide conjugated to this site. The mPEG-hIL-11 conjugate was purified and showed a single band on SDS-PAGE with an apparent molecular weight. The biological activity of purified mPEG-hIL-11 was determined using a dependent cell line 7TD1. The remaining biological activity of PEGylated-rhIL-11 was 30% of native rhIL-11, suggesting chemical modification of rhIL-11 by PEG is a promising approach for improving the pharmacological efficacy.



Key wordshuman interleukin-11(hIL11);Polyethylene glycol;Chemical modification     
Received: 16 February 2009      Published: 02 July 2009
Cite this article:

LI Zhi-Hua- Hu-Man-Cang- Yan-Ling-Mei- Diao-Yu-Jiao- Yang-Xu- Bang-Zheng-Hua- Xu-Wei-Meng- Li-Jian-Feng. Site-specific PEGylation of engineered cysteine analogues of recombinant human interleukin-11. China Biotechnology, 2009, 29(06): 20-24.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2009/V29/I06/20

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