Expression and Purification of Human Parathyroid Hormone Peptide(1-34) in Escherichia coli / 中国生物工程杂志
China Biotechnology
;
(12)2006.
Article
in Chinese
| WPRIM
| ID: wpr-684889
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.
Full text:
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Index:
WPRIM (Western Pacific)
Language:
Chinese
Journal:
China Biotechnology
Year:
2006
Type:
Article
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