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中国生物工程杂志

China Biotechnology
China Biotechnology  2010, Vol. 30 Issue (03): 74-78    DOI:
    
Expression and Purification of Fusion Protein with SUMO of Human Epidermal Growth Factor
1.College of Life Sciences, Jilin Agricultural University, Changchun 130118, China
2.Engineering Research Center of Bioreactor and Pharmaceutical Development, Ministry of Education, Jilin Agricultural University,Changchun 130118, China
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Abstract  

The condition of both expression and purification of SUMO human epidermal growth factor in E.coli is discussed. After transforming recombinant expression vector into E.coli, the experiment optimizes the induction expression, and analysis through ion exchange chromatography NiNTA affinity chromatography and molecular sieve chromatography, adopting arabinose as the IPTG. The results are as follows: 37℃ is the most favorable temperature for induction expression of SUMO-hEGF in BL21(AI), 5.0g/L the most best concentration of arabinose, and 4h the best  time for induction expression. Meanwhile, the quantity of expression is around 20.2%. The conclusion that hEGF is the purified protein is verified by Western blot.The good foundation for the development of hEGF genetic medicine is founded.



Key wordsHuman Epidermal Growth Factor (hEGF)      arabinose      SUMO      Purification     
Received: 16 December 2009      Published: 25 March 2010
Cite this article:

ZHANG Hai-Miao, LIU Xiao-Ju, TIAN Hai-Shan, MO Xiao-Shan, DENG Lin, LI Jiao-Kun. Expression and Purification of Fusion Protein with SUMO of Human Epidermal Growth Factor. China Biotechnology, 2010, 30(03): 74-78.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2010/V30/I03/74

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