Purification and characterization of native human elongation factor 2

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DOI

  • 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.

OriginalsprogEngelsk
TidsskriftProtein Expression and Purification
Vol/bind158
Sider (fra-til)15-19
Antal sider5
ISSN1046-5928
DOI
StatusUdgivet - 1 jun. 2019

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