Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli

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• 作者：Chunfang Ling (1) (2)
  Junyan Zhang (2)
  Deqiu Lin (1) (2)
  Ailin Tao (2)
  
  1. School of Life Science ; South China Normal University ; 55# Zhongshan Road West ; Tianhe District ; Guangzhou ; 510631 ; People鈥檚 Republic of China
  2. Guangdong Provincial Key Laboratory of Allergy & Clinical Immunology ; The State Key Laboratory of Respiratory Disease ; The Second Affiliated Hospital of Guangzhou Medical University ; 250# Changgang Road East ; Guangzhou ; 510260 ; Guangdong Province ; People鈥檚 Republic of China
  
• 关键词：Papain ; like cysteine proteases ; Escherichia coli ; Refolding ; Purification ; Activation
• 刊名：World Journal of Microbiology & Biotechnology
• 出版年：2015
• 出版时间：May 2015
• 年：2015
• 卷：31
• 期：5
• 页码：681-690
• 全文大小：292 KB
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• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Applied Microbiology
  Biotechnology
  Biochemistry
  Environmental Biotechnology
  Microbiology
  
• 出版者：Springer Netherlands
• ISSN：1573-0972

文摘

Papain-like cysteine proteases are widely expressed, fulfill specific functions in extracellular matrix turnover, antigen presentation and processing events, and may represent viable drug targets for major diseases. In depth and rigorous studies of the potential for these proteins to be targets for drug development require sufficient amounts of protease protein that can be used for both experimental and therapeutic purposes. Escherichia coli was widely used to express papain-like cysteine proteases, but most of those proteases are produced in insoluble inclusion bodies that need solubilizing, refolding, purifying and activating. Refolding is the most critical step in the process of generating active cysteine proteases and the current approaches to refolding include dialysis, dilution and chromatography. Purification is mainly achieved by various column chromatography. Finally, the attained refolded proteases are examined regarding their protease structures and activities.