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[Purification of recombinant hEGF expressed in yeast Pichia pastoris and the study on its characters]
1National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS, PUMC, Beijing 100005, China. huangbr@public.bta.net.cn
Objective:
To obtain recombinant human epidermal growth factor(hEGF) that can be used in animal experiments and clinical trial.
Method:
Chemically synthesized hEGF gene was expressed in Yeast Pichia pastoris and the secretory hEGF was purified by Phenysepharose 6 Fast Flow(high sub), Q-sepharose High Performance, and Superdex 30 chromatography, and its characters were studied by respective methods.
Results:
The purified hEGF doesn't contain pyrogen, endotoxin, or yeast chromosome DNA and the purity reached 98%. The recombinant human EGF has correct molecular weight, pI, N-terminal amino acids sequences, peptide map, ultraviolet spectrum and well-biological activity.
Conclusion:
The purified hEGF is in accord with the requirements for animal experiments and clinical trial which provides the basis of preparing EGF agents for clinical test.