[Purification of recombinant hEGF expressed in yeast Pichia pastoris and the study on its characters].
作者信息
Huang B R, Cai L W, Wang X, Ma X M, Ma X L, Li J J, Li H Z, Wei Z M, Liang Q, Zheng H J, Tang Q H, Tang S X, Liao H T, Xiang X Z
机构信息
National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS, PUMC, Beijing 100005, China.
出版信息
Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 2001 Apr;23(2):106-10.
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.
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