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Soluble expression of a synthetic gene for human translation initiation factor 4E in Escherichia coli.

Authors :
Morino S
Teraoka Y
Doi M
Ishida T
Ueda H
Uesugi S
Source :
Biological & pharmaceutical bulletin [Biol Pharm Bull] 1995 Feb; Vol. 18 (2), pp. 372-6.
Publication Year :
1995

Abstract

In order to obtain the active form of recombinant human initiation factor (eIF) 4E effectively, an artificial synthetic gene was cloned into an expression vector (pMAL-p2) and the soluble expression was attempted in Escherichia coli under the control of a tac promoter. Two expression systems were finally constructed as a fusion protein with maltose-binding protein, which contain a recognition sequence for the site specific protease alpha-thrombin and factor Xa, respectively. Most of the fusion protein was induced as a soluble form. The soluble human eIF-4E digested from the fusion protein showed binding specificity for the m7GTP affinity column.

Details

Language :
English
ISSN :
0918-6158
Volume :
18
Issue :
2
Database :
MEDLINE
Journal :
Biological & pharmaceutical bulletin
Publication Type :
Academic Journal
Accession number :
7742816
Full Text :
https://doi.org/10.1248/bpb.18.372