Cloning, expression and purification of human epidermal growth factor using different expression systems

L. Ferrer Soler, J. Cedano, E. Querol, R. De Llorens

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18 Citations (Scopus)

Abstract

Epidermal growth factor (EGF) is a protein that belongs to the family of growth factors that bind the ErbB receptors, which play a prominent role in the development of carcinomas. We had demonstrated that potato carboxypeptidase inhibitor (PCI) acts as an EGF antagonist. Because of the low affinity of PCI for the epidermal growth factor receptor, it was decided to design EGF mutants with PCI abilities. In order to achieve this we have first cloned, expressed and purified the native protein, EGF. Different expression systems with different locations of the recombinant protein were designed and a purification protocol was designed with those which allowed expression of EGF. Finally, the sample needed folding. Differences in the amount of EGF obtained and its activity were observed depending on the expression system used. © 2003 Elsevier Science B.V. All rights reserved.
Original languageEnglish
Pages (from-to)113-123
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume788
Issue number1
DOIs
Publication statusPublished - 5 May 2003

Keywords

  • Cloning
  • Epidermal growth factor
  • Expression
  • Purification

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