PTD-hEGF fusion protein--gene expression and function analysis.
- Author:
Qing-Wen ZHI
1
;
Shu-Hao WANG
;
Feng-Ying ZHANG
;
Shi-Gui LI
;
Man-Ji SUN
Author Information
1. Institute of Pharmacology and Toxicology, Academy of Military Medical Sciences, Beijing 100850, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Cell Line;
Cell Proliferation;
drug effects;
Epidermal Growth Factor;
biosynthesis;
genetics;
Escherichia coli;
genetics;
metabolism;
Humans;
Molecular Sequence Data;
Recombinant Fusion Proteins;
biosynthesis;
genetics;
pharmacology;
Transduction, Genetic
- From:
Chinese Journal of Biotechnology
2007;23(4):589-592
- CountryChina
- Language:Chinese
-
Abstract:
To produce membrane-permeable human epidermal growth factor (hEGF), a pPTD-hEGF prokaryocyte expression vector was constructed and transformed into E. coli BL 21 (DE3). The PTD-hEGF fusion protein was induced by 0.3 mmol/L of IPTG expressed in the form of inclusion body with an yield of 40% of the total protein in the cells, and then purified by Ni2+ -NTA affinity chromatography. The SDS-PAGE analysis showed a single fusion protein band with a molecular weight of 16 kD. The amino acid sequence was checked by MALDI-TOF-MS analysis. The genetic engineering PTD-hEGF fusion protein obviously promoted the proliferation and growth of the HEK-293 cells in vitro.
