Expression of recombinant human epidermal growth factor in Escherichia coli and characterization of its biological activity.
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.
Department of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia. ahmadfaizal2003@yahoo.com
Ahmad Faizal
AF
Abdull Razis
Elysha Nur
EN
Ismail
Zarida
Z
Hambali
Muhammad Nazrul Hakim
MN
Abdullah
Abdul Manaf
AM
Ali
Mohd Azmi
MA
Mohd Lila
D049109:Cell Proliferation / Q000187:drug effects; D020405:Dermis / Q000166:cytology; D004797:Enzyme-Linked Immunosorbent Assay; D004815:Epidermal Growth Factor / Q000032:analysis / Q000096:biosynthesis* / Q000235:genetics / Q000494:pharmacology*; D004926:Escherichia coli / Q000166:cytology / Q000235:genetics*; D005347:Fibroblasts / Q000166:cytology / Q000187:drug effects; D015870:Gene Expression; D006801:Humans; D015151:Immunoblotting; D019897:Periplasm / Q000378:metabolism; D011994:Recombinant Proteins / Q000032:analysis / Q000096:biosynthesis* / Q000235:genetics / Q000494:pharmacology*; D013997:Time Factors
D011994:Recombinant Proteins; D004815:Epidermal Growth Factor