Engineering of a System for the Production of Mutant Human Alpha-Fetoprotein in the Methylotrophic Yeast Pichia pastoris

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• 作者：E. V. Morozkina ; E. A. Vavilova ; S. S. Zatcepin…
• 关键词：recombinant human alpha ; fetoprotein ; Pichia pastoris ; antitumor therapy
• 刊名：Applied Biochemistry and Microbiology
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：52
• 期：2
• 页码：170-175
• 全文大小：538 KB
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• 作者单位：E. V. Morozkina (1)
  E. A. Vavilova (1)
  S. S. Zatcepin (1)
  E. V. Klyachko (1)
  T. A. Yagudin (1)
  A. M. Chulkin (1)
  I. V. Dudich (2)
  L. N. Semenkova (2)
  I. V. Churilova (3)
  S. V. Benevolensky (1)
  
  1. Bach Institute of Biochemistry, Fundamental Principles of Biotechnology, Federal Research Center, Russian Academy of Sciences, Moscow, 119071, Russia
  2. Institute of Engineering Immunology, Lyubuchany, Moscow region, 142380, Russia
  3. Enzyme Technologies, St. Petersburg, 197110, Russia
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Microbiology
  Medical Microbiology
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3024

文摘

A system for the production of mutant recombinant human alpha-fetoprotein (rhAFP0) lacking the glycosylation site has been engineered in the yeast Pichia pastoris. A strain of the methylotrophic yeast Pichia pastoris GS115/pPICZαA/rhAFP0, which produces unglycosylated rhAFP0 and secretes it to the culture medium, has been constructed. Optimization and scale-up of the fermentation technology have resulted in an increase in the rhAFP0 yield to 20 mg/L. A scheme of isolation and purification of biologically active rhAFP0 has been developed. The synthesized protein has the antitumor activity, which is analogous to the activity of natural human embryonic alpha-fetoprotein.