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Updated: Aug 17, 2026

Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
[High expression and characterization of human parathyroid hormone in Escherichia coli]
Hong-Qing Fang1, Hong-Mei Dai, Yan-Ying Li
1Beijing Institute of Biotechnology, Beijing 100071, China. fanghongqing@hotmail.com
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.
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