High expression and characterization of human parathyroid hormone in Escherichia coli.
- Author:
Hong-Qing FANG
1
;
Hong-Mei DAI
;
Yan-Ying LI
;
Hong-Liang ZHAO
;
Bing-Bing DENG
;
Chong XUE
;
Zhi-Min LIU
;
Hou-Chu ZHU
;
Qing-Jun MA
;
Hui-Peng CHEN
Author Information
1. Beijing Institute of Biotechnology, Beijing 100071, China. fanghongqing@hotmail.com
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Animals;
Base Sequence;
Bone Density;
drug effects;
Chromatography, Ion Exchange;
Electrophoresis, Polyacrylamide Gel;
Escherichia coli;
genetics;
metabolism;
Female;
Humans;
Molecular Sequence Data;
Ovariectomy;
Parathyroid Hormone;
chemistry;
genetics;
metabolism;
pharmacology;
Rats;
Rats, Wistar;
Sequence Alignment;
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- From:
Chinese Journal of Biotechnology
2003;19(1):102-106
- CountryChina
- Language:Chinese
-
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.
