Purification of Recombinant hEGF Expressed in Yeast Pichia pastoris and the Study on Its Characters
- VernacularTitle:甲基营养型酵母系统表达的重组人表皮生长因子的纯化及其性质
- Author:
Bing-Ren HUANG
1
;
Liang-Wan CAI
;
Xin WANG
;
Xue-Mei MA
;
Xiao-Li MA
;
Jing-Jun LI
;
Hong-Zhuo LI
;
Zhong-Ming WEI
;
Qing LIANG
;
Hua-Jun ZHENG
;
Qi-Hac TANG
;
Sheng-Xiu TANG
;
Hong-Tao LIAO
;
Xu-Zhuan XIANG
Author Information
1. CAMS and PUMC
- From:
Acta Academiae Medicinae Sinicae
2001;23(2):106-110
- CountryChina
- Language:Chinese
-
Abstract:
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 se quences, 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 provids the basis of prepar ing EGF agents for clinical test.
