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中国生物工程杂志

China Biotechnology
China Biotechnology  2012, Vol. 32 Issue (04): 1-6    DOI:
    
Expression and Purification of Recombinant AgrC and Construction of Its Artificial Supramolecular System
LIU Chun-guang1,2, QUAN Chun-shan2, WANG Jian-feng2, YU Gui-mei2, FAN Sheng-di2
1. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China;
2. Key Laboratory of Biochemical Engineering, State Ethnic Affairs Commission and Ministy of Education Dalian Nationalities University, Dalian 116600, China
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Abstract  

Objective: To express and purify AgrC, a receptor protein of Staphylococcus aureus and to construct its artificial supramolecular system. Methods: AgrC expression bacterial strain, E. coli TOP10-pBAD-AgrC was constructed. The induction conditions and the extracting methods of the protein were optimized. The recombinant protein was identified by Western blot and purified with HisTrap affinity column. The vesicle was prepared with peptide lipid N+C5Gly2C16, and the purified protein was subsequently inset into the vesicle. Results: The constructed engineering bacterium had an optimal expression at 18℃ and with 0.002% arabinose. The protein existing in membrane was maximally dissoluted with BDH. Conclusion: The recombinant AgrC was expressed and purified successfully, and an artificial supramolecular system was constructed.



Key wordsStaphylococcus aureus      Artificial supramolecular system      Vesicle     
Received: 16 January 2012      Published: 25 April 2012
ZTFLH:  Q819  
Cite this article:

LIU Chun-guang, QUAN Chun-shan, WANG Jian-feng, YU Gui-mei, FAN Sheng-di. Expression and Purification of Recombinant AgrC and Construction of Its Artificial Supramolecular System. China Biotechnology, 2012, 32(04): 1-6.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2012/V32/I04/1


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