In vitro refolding with simultaneous purification of recombinant human parathyroid hormone (rhPTH 1᾿4) from Escherichia coli directed by protein folding size exclusion chromatography (PF-SEC): implication of solution additi

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• 作者：Sandeep Vemula ; Sushma Vemula ; Akshay Dedaniya…
• 关键词：PFLC ; Size exclusion chromatography ; Purity ; Recovery yield ; Specific activity ; rhPTH
• 刊名：Analytical and Bioanalytical Chemistry
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：408
• 期：1
• 页码：217-229
• 全文大小：2,021 KB
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• 作者单位：Sandeep Vemula (1)
  Sushma Vemula (2)
  Akshay Dedaniya (1)
  Srinivasa Reddy Ronda (1)
  
  1. Centre for Bioprocess Technology, Department of Biotechnology, K L E F University, Green Fields, Vaddeswaram, Guntur, 522 502, Andhra Pradesh, India
  2. Department of Pharmacology, Kakatiya University, Vidyaranyapuri, Hanamkonda, Warangal, Telangana, 506009, India
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Analytical Chemistry
  Food Science
  Inorganic Chemistry
  Physical Chemistry
  Monitoring, Environmental Analysis and Environmental Ecotoxicology
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1618-2650

文摘

Recombinant proteins are frequently hampered by aggregation during the refolding and purification process. A simple and rapid method for in vitro refolding and purification of recombinant human parathyroid hormone (rhPTH 1–34) expressed in Escherichia coli with protein folding size exclusion chromatography (PF-SEC) was developed in the present work. Discrete effects of potential solution additives such as urea, polypolyethylene glycol, proline, and maltose on the refolding with simultaneous purification of rhPTH were investigated. The results of individual additives indicated that both maltose and proline had remarkable influences on the efficiency of refolding with a recovery yield of 65 and 66 % respectively. Further, the synergistic effect of these additives on refolding was also explored. These results demonstrate that the additive combinations are more effective for inhibiting protein aggregation during purification of rhPTH in terms of recovery yield, purity, and specific activity. The maltose and proline combination system achieved the highest renatured rhPTH having a recovery yield of 78 %, a purity of ≥99 %, and a specific activity of 3.31 × 103 cAMP pM/cell respectively, when compared to the classical dilution method yield (41 %) and purity (97 %). In addition, the role of maltose and proline in a combined system on protein aggregation and refolding has been explained. The molecular docking (in silico) scores of maltose (−10.91) and proline (−9.0) support the in vitro results.