[Purification of recombinant hEGF expressed in yeast Pichia pastoris and the study on its characters].
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.