Expression vector promoting the synthesis and export of the human growth-hormone-releasing factor in Escherichia coli
| Autor: | Willem Roskam, Claude Lazdunski, Roland Lloubès, Jamila Anba, Jean-Marie Pagès, Evelyne Joseph-Liauzun, Daniel Baty, David Shire |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Recombinant Fusion Proteins
Two-hybrid screening Genetic Vectors Biology medicine.disease_cause law.invention Methionine Plasmid Bacterial Proteins law Gene expression Escherichia coli Genetics medicine Humans Cyanogen Bromide Promoter Regions Genetic Expression vector Binding protein Biological Transport General Medicine Periplasmic space Phosphate-Binding Proteins Molecular Weight Biochemistry Growth Hormone Recombinant DNA Carrier Proteins Protein Processing Post-Translational |
| Zdroj: | Gene. 53:219-226 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/0378-1119(87)90010-2 |
| Popis: | We have studied the synthesis, processing and export of human growth-hormone-releasing factor (hGRF) in Escherichia coli transformed with a plasmid constructed for the expression of hGRF as a hybrid protein. A DNA fragment containing the entire sequence of phosphate-binding protein gene (phoS) is fused to a modified hGRF-coding sequence (phoS-mhGRF). The hybrid protein, PhoS-mhGRF, was recovered in the supernatant fluid after spheroplasting treatment indicating correct export to the periplasmic space. Pulse-chase experiments demonstrated that the hybrid protein was similarly processed as the PhoS precursor. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|