Expression vector promoting the synthesis and export of the human growth-hormone-releasing factor in Escherichia coli
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 f...
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Veröffentlicht in: | Gene 1987, Vol.53 (2), p.219-226 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 0378-1119 1879-0038 |
DOI: | 10.1016/0378-1119(87)90010-2 |