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The Scientific World Journal - Volume 2014 2014, Article ID 830923, 6 pages -

Research Article

Centre of Biotechnology of Sfax, P.O. Box 1177, 3018 Sfax, Tunisia

Instituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científica and Universidad Autónoma de Madrid, Arturo Duperier 4, 28029 Madrid, Spain

Received 4 April 2014; Revised 25 July 2014; Accepted 28 July 2014; Published 15 October 2014

Academic Editor: Adhar C. Manna

Copyright © 2014 Jihene Elloumi-Mseddi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Our success in producing an active epidermal growth factor receptor EGFR tyrosine kinase in Escherichia coli encouraged us to express the full-length receptor in the same host. Despite its large size, we were successful at producing the full-length EGFR protein fused to glutathione S-transferase GST that was detected by Western blot analysis. Moreover, we obtained a majoritarian truncated GST-EGFR form detectable by gel electrophoresis and Western blot. This truncated protein was purified and confirmed by MALDI-TOF-TOF analysis to belong to the N-terminal extracellular region of the EGFR fused to GST. Northern blot analysis showed two transcripts suggesting the occurrence of a transcriptional arrest.





Autor: Jihene Elloumi-Mseddi, Karim Jellali, Antonio Villalobo, and Sami Aifa

Fuente: https://www.hindawi.com/



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