Purification and characterization of native human elongation factor 2

Rasmus Kock Flygaard; Beatrice Malacrida; Patrick Kiely; Lasse Bohl Jenner

doi:10.1016/j.pep.2019.02.005

Purification and characterization of native human elongation factor 2

Rasmus Kock Flygaard, Beatrice Malacrida, Patrick Kiely, Lasse Bohl Jenner^*

^*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Abstract

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 language	English
Journal	Protein Expression and Purification
Volume	158
Pages (from-to)	15-19
Number of pages	5
ISSN	1046-5928
DOIs	https://doi.org/10.1016/j.pep.2019.02.005
Publication status	Published - 1 Jun 2019

Keywords

Human eEF2
Translation

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10.1016/j.pep.2019.02.005

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title = "Purification and characterization of native human elongation factor 2",

abstract = "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.",

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author = "Flygaard, {Rasmus Kock} and Beatrice Malacrida and Patrick Kiely and Jenner, {Lasse Bohl}",

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T1 - Purification and characterization of native human elongation factor 2

AU - Flygaard, Rasmus Kock

AU - Malacrida, Beatrice

AU - Kiely, Patrick

AU - Jenner, Lasse Bohl

PY - 2019/6/1

Y1 - 2019/6/1

N2 - 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.

AB - 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.

KW - Human eEF2

KW - Translation

UR - http://www.scopus.com/inward/record.url?scp=85061365020&partnerID=8YFLogxK

U2 - 10.1016/j.pep.2019.02.005

DO - 10.1016/j.pep.2019.02.005

M3 - Journal article

C2 - 30742898

AN - SCOPUS:85061365020

SN - 1046-5928

VL - 158

SP - 15

EP - 19

JO - Protein Expression and Purification

JF - Protein Expression and Purification

ER -

Purification and characterization of native human elongation factor 2

Abstract

Keywords

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