[High expression and characterization of human parathyroid hormone in Escherichia coli].
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.
Fang
Hong-Qing
HQ
Beijing Institute of Biotechnology, Beijing 100071, China. fanghongqing@hotmail.com
Dai
Hong-Mei
HM
Li
Yan-Ying
YY
Zhao
Hong-Liang
HL
Deng
Bing-Bing
BB
Xue
Chong
C
Liu
Zhi-Min
ZM
Zhu
Hou-Chu
HC
Ma
Qing-Jun
QJ
Chen
Hui-Peng
HP
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015519:Bone Density / Q000187:drug effects; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005260:Female; D006801:Humans; D008969:Molecular Sequence Data; D010052:Ovariectomy; D010281:Parathyroid Hormone / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D051381:Rats; D017208:Rats, Wistar; D016415:Sequence Alignment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D010281:Parathyroid Hormone