Purification and characterization of native human elongation factor 2

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Rasmus Kock Flygaard
  • Beatrice Malacrida, University of Limerick, Graduate Entry Medical School, University of Limerick
  • ,
  • Patrick Kiely, University of Limerick, Graduate Entry Medical School, University of Limerick
  • ,
  • Lasse Bohl Jenner, Université Louis Pasteur

Human elongation factor 2 is the translocase that is responsible for the movement of tRNA from the A- to P- and P- to E-site on the ribosome during the elongation phase of translation. Being a vital factor of protein biosynthesis, its function is highly controlled and regulated. It has been implicated in numerous diseases and pathologies, and as such it is important to have a source for isolated pure and active protein for biomedical and biochemical studies. Here we report development of a purification protocol for native human elongation factor 2 from HEK-293S cells. The resulting protein is active, pure, has an intact diphtamide and is obtainable in yields suitable for functional and structural studies.

Original languageEnglish
JournalProtein Expression and Purification
Volume158
Pages (from-to)15-19
Number of pages5
ISSN1046-5928
DOIs
Publication statusPublished - 1 Jun 2019

    Research areas

  • Human eEF2, Translation

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