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Functional solubilization of aggregation-prone TRAIL protein facilitated by coexpressing with protein isoaspartate methyltranferase
- Source :
- Applied microbiology and biotechnology. 72(5)
- Publication Year :
- 2006
-
Abstract
- TRAIL was a tumor-specific protein in development as a novel anticancer therapeutic agent. Generally, when expressed in recombinant Escherichia coli, TRAIL protein was prone to form inclusion bodies. In this study, coexpression of human TRAIL protein and protein isoaspartate methyltranferase (PIMT) from E. coli on plasmid pBV-TRAIL-PCM in E. coli C600 was investigated to overcome the difficulties in soluble expression. The results showed that this PIMT coexpression strategy exerted a positive effect on the TRAIL protein expression in recombinant E. coli, which led to a mean increase in the intracellular concentration of soluble and total protein of TRAIL by 1.57-fold and 1.33-fold, respectively. At the same time, results also suggested that PIMT was a prospective partner for soluble expression of TRAIL protein.
- Subjects :
- General Medicine
Isomerase
Biology
medicine.disease_cause
Applied Microbiology and Biotechnology
Inclusion bodies
law.invention
Isoaspartate
TNF-Related Apoptosis-Inducing Ligand
Plasmid
TRAIL Protein
Biochemistry
law
Fermentation
Protein D-Aspartate-L-Isoaspartate Methyltransferase
medicine
Recombinant DNA
Escherichia coli
Cloning, Molecular
Intracellular
Biotechnology
Subjects
Details
- ISSN :
- 01757598
- Volume :
- 72
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Applied microbiology and biotechnology
- Accession number :
- edsair.doi.dedup.....d5cbbcd1b6849f838668765b945d9903