Expression of Recombinant Human Epidermal Growth Factor in Escherichia coli and Characterization of its Biological Activity
| Autor: | Zarida Hambali, Muhammad Nazrul Hakim Abdullah, Ahmad Faizal Abdull Razis, Abdul Manaf Ali, Elysha Nur Ismail, Mohd Azmi Mohd Lila |
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| Rok vydání: | 2007 |
| Předmět: |
Time Factors
Immunoblotting Cell Gene Expression Enzyme-Linked Immunosorbent Assay Bioengineering Biology medicine.disease_cause Applied Microbiology and Biotechnology Biochemistry law.invention Epidermal growth factor law Escherichia coli medicine Humans Molecular Biology Cell Proliferation Epidermal Growth Factor Cell growth Biological activity Dermis General Medicine Fibroblasts Fusion protein Recombinant Proteins In vitro medicine.anatomical_structure Periplasm Recombinant DNA Biotechnology |
| Zdroj: | Applied Biochemistry and Biotechnology. 144:249-261 |
| ISSN: | 1559-0291 0273-2289 |
| Popis: | Recombinant human epidermal growth factor (EGF) was successfully expressed as a fusion protein in Escherichia coli system. This system was used OmpA signal sequence to produce soluble protein into the periplasm of E. coli. Human EGF (hEGF) synthesized in bacterial cell was found to be similar in size with the original protein and molecular weight approximately at 6.8 kDa. Cell proliferation assay was conducted to characterize the biological activity of hEGF on human dermal fibroblasts. The synthesized hEGF was found to be functional as compared with authentic hEGF in stimulating cell proliferation and promoting growth of cell. In comparison of biological activity between synthesized and commercial hEGF on cell proliferation, the results showed there was no significant different. This finding indicates the synthesized hEGF in E. coli system is fully bioactive in vitro. |
| Databáze: | OpenAIRE |
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