毕赤酵母表达重组人白细胞介素11的纯化与鉴定

报道了毕赤酵母表达人白细胞介素11的下游工艺研究，并对其产物进行了分析鉴定。所用工艺流程为离心收集上清、超滤浓缩脱盐、离子交换层析、疏水层析、凝胶过滤。所得产物经SDSPAGE电泳、RPHPLC分析、N端和C端序列分析、质谱、等电点分析和生物学活性分析，结果表明：产品纯度大于97%，结构和性质与E.coli融合表达的Neumega完全一致。

Purification and Characterization of Recombinant Human Interleukin 11 Which Expressed by Pichia pastoris

This study first time report a method to purify the rhIL|11 which expressed by %Pichia pastoris%.rhIL|11 was secreted into the supernatant and collected by centrifugation.The purity of rhIL|11 reached 97% through the steps of ultrafiltration,SP Sepharose FF,Phenyl Sepharose HP and Sephadex G25.Analysis of SDS|PAGE,Western|blotting,IEF,RP HPLC,Mass spectrometer,N and C terminus amino acid sequence and bioactivity was conducted.All the analysis results proved that the rhIL|11 expressed by %Pichia pastoris %was the same as Neumeg which was expressed in %E.coli% with fusion expression system.So it is possibly a cheaper and easilier method to produce rhIL|11 for clinical use.