High Expression and Characterization of Human Parathyroid Hormone in Escherichia coli
人甲状旁腺激素在大肠杆菌中的表达及鉴定

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.