High-level secretion of human growth hormone by Escherichia coli
| Autor: | Herbert L. Heyneker, Barry Ronald Bochner, Gregory L. Gray, Chung-Nan Chang, Michael W. Rey |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Signal peptide
Recombinant Fusion Proteins Genetic Vectors Protein Sorting Signals Regulatory Sequences Nucleic Acid Biology medicine.disease_cause Chorionic Gonadotropin Gene expression Escherichia coli Genes Synthetic Genetics medicine Humans Secretion Promoter Regions Genetic Gene General Medicine Periplasmic space Molecular biology Recombinant Proteins Genes Regulatory sequence bacteria Alkaline phosphatase Protein Processing Post-Translational |
| Zdroj: | Gene. 55:189-196 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/0378-1119(87)90279-4 |
| Popis: | A gene encoding the mature form of human growth hormone (hGH) was fused to the secretion signal coding sequence of the Escherichia coli heat-stable enterotoxin II (STII). This hybrid gene was preceded by two Shine-Dalgarno sequences derived from the trp and STII-coding genes and was expressed in E. coli under the transcriptional control of the E. coli alkaline phosphatase (phoA) promoter. In low-phosphate growth media, cells synthesized about 15 to 25 micrograms of hGH/ml/1 A550 unit of cells. This represents 6 to 10% of total cellular protein. The majority of the hGH produced (more than 90%) was processed precisely and secreted into the periplasmic space. These results demonstrate that E. coli cells are able to synthesize and secrete high levels of this human protein using a prokaryotic signal sequence. |
| Databáze: | OpenAIRE |
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