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Purification and characterization of native human elongation factor 2

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posted on 2019-02-22, 14:27 authored by Rasmus Kock Flygaard, Beatrice Malacrida, Patrick A. Kiely, Lasse Bohl Jenner
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.

History

Publication

Protein Expression and Purification;158, pp. 15-19

Publisher

Elsevier

Note

peer-reviewed

Rights

This is the author’s version of a work that was accepted for publication in Protein Expression and Purification . Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Protein Expression and Purification, 2019, 158, pp. 159-19, https://doi.org/10.1016/j.pep.2019.02.005

Language

English

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