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Soluble expression of a synthetic gene for human translation initiation factor 4E in Escherichia coli.
- 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.
- Subjects :
- Amino Acid Sequence
Base Sequence
Chromatography, Affinity
Cloning, Molecular
DNA Primers
Electrophoresis, Polyacrylamide Gel
Eukaryotic Initiation Factor-4E
Gene Expression
Humans
Molecular Sequence Data
Peptide Initiation Factors isolation & purification
Plasmids
Promoter Regions, Genetic
Protein Binding
Recombinant Proteins genetics
Recombinant Proteins isolation & purification
Escherichia coli genetics
Genes, Synthetic
Peptide Initiation Factors genetics
Subjects
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