The conditions of fermentation for recombinant neurotoxins tranfering into P Pastoris GS 11.5 and their further purification procedures were investigated. An identification of the target protein was carried out with the SDS-PAGE electrophoresis and its productivity reached 350mg/L. After the purification procedures including the ultra filtration, ion-exchange chromatography and the gel filtration were performed, the purity of the product, which was analyzed by HPLC, was 92%.
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References
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