【摘要】 化学合成人甲状旁腺激素 (hPTH)全长基因 ,克隆到大肠杆菌表达载体pBV2 2 0和pET2 2b中 ,获得了高表达。经破菌、阳离子交换层析、反相层析纯化获得了纯度大于 95 %的纯品。N端测序、质谱分析结果表明重组hPTH结果完整 ,N端无Met或fMet。生物活性试验证明重组hPTH具有激活腺苷酸环化酶、增加骨质量和骨密度等作用。更多还原

【Abstract】 Human parathyroid hormone(hPTH) was highly expressed in Escherichia coli by inserted the synthesized whole hPTH cDNA into the vectors pBV220 and pET22b.After expression and disruption,the purified product was acquired through cation exchange chromatography and reverse phase chromatography.From the results of N terminal sequencing and MALDI TOF MS analysis the recombiant prtein was indentified as intact hPTH.In in vitro Bioassays the recombinant hPTH stimulated adenylate cyclase as the standard did. In ovariectomized rats the recombinant hPTH markedly increased the femoral bone mass and bone mineral density.更多还原