毕赤酵母表达重组人白细胞介素11的纯化与鉴定

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

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 .

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.