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Purification and characterization of native human elongation factor 2

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Purification and characterization of native human elongation factor 2. / Flygaard, Rasmus Kock; Malacrida, Beatrice; Kiely, Patrick; Jenner, Lasse Bohl.

I: Protein Expression and Purification, Bind 158, 01.06.2019, s. 15-19.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Flygaard, RK, Malacrida, B, Kiely, P & Jenner, LB 2019, 'Purification and characterization of native human elongation factor 2', Protein Expression and Purification, bind 158, s. 15-19. https://doi.org/10.1016/j.pep.2019.02.005

APA

Flygaard, R. K., Malacrida, B., Kiely, P., & Jenner, L. B. (2019). Purification and characterization of native human elongation factor 2. Protein Expression and Purification, 158, 15-19. https://doi.org/10.1016/j.pep.2019.02.005

CBE

Flygaard RK, Malacrida B, Kiely P, Jenner LB. 2019. Purification and characterization of native human elongation factor 2. Protein Expression and Purification. 158:15-19. https://doi.org/10.1016/j.pep.2019.02.005

MLA

Flygaard, Rasmus Kock o.a.. "Purification and characterization of native human elongation factor 2". Protein Expression and Purification. 2019, 158. 15-19. https://doi.org/10.1016/j.pep.2019.02.005

Vancouver

Flygaard RK, Malacrida B, Kiely P, Jenner LB. Purification and characterization of native human elongation factor 2. Protein Expression and Purification. 2019 jun 1;158:15-19. https://doi.org/10.1016/j.pep.2019.02.005

Author

Flygaard, Rasmus Kock ; Malacrida, Beatrice ; Kiely, Patrick ; Jenner, Lasse Bohl. / Purification and characterization of native human elongation factor 2. I: Protein Expression and Purification. 2019 ; Bind 158. s. 15-19.

Bibtex

@article{403d94579cb0408f8098d7bfa83f7825,
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.",
keywords = "Human eEF2, Translation",
author = "Flygaard, {Rasmus Kock} and Beatrice Malacrida and Patrick Kiely and Jenner, {Lasse Bohl}",
year = "2019",
month = jun,
day = "1",
doi = "10.1016/j.pep.2019.02.005",
language = "English",
volume = "158",
pages = "15--19",
journal = "Protein Expression and Purification",
issn = "1046-5928",
publisher = "Academic Press",

}

RIS

TY - JOUR

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

VL - 158

SP - 15

EP - 19

JO - Protein Expression and Purification

JF - Protein Expression and Purification

SN - 1046-5928

ER -