Expression and Purification of Human Parathyroid Hormone Peptide(1-34) in Escherichia coli
- VernacularTitle:重组人甲状旁腺激素肽(1-34)在大肠杆菌中的高效融合表达及纯化
- Author:
Jian-Feng LI
;
Hong-Jian XIAO
;
Qiu-Yan JI
;
Zhi-Hua LI
;
Hai-Ting LONG
;
Ling-Mei YAN
;
Na LUO
;
Wei-Ming XU
;
- Publication Type:Journal Article
- Keywords:
Human parathyroid hormone Escherichia coli Fusion expression
- From:
China Biotechnology
2006;0(03):-
- CountryChina
- Language:Chinese
-
Abstract:
Human parathyroid hormone peptide1-34(hPTH1-34) was highly expressed in Escherichia coli by inserting the synthesized hPTH1-34 cDNA into pThioHis, the prokaryotic expression vector. The expressed hPTH1-34 was purified by chelating sepharose immobilized metal ion affinity, reverse and filter chromatographic steps. Its purity was verified above 95% by HPLC. The quality was identified by N-terminal sequencing and MALDI-TOF-MS analysis. In vitro analysis showed the adenylate cyclase of ROS 17/2.8 cells was activated by hPTH1-34.
