Expression and Purification of Human Parathyroid Hormone Peptide（1-34） in Escherichia coli

China Biotechnology

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Expression and Purification of Human Parathyroid Hormone Peptide（1-34） in Escherichia coli

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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.

Key words： Escherichia coli Fusion expression Human parathyroid hormone

Received: 10 February 2006 Published: 25 March 2006

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. Expression and Purification of Human Parathyroid Hormone Peptide（1-34） in Escherichia coli. China Biotechnology, 2006, 26(03): 26-30.

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https://manu60.magtech.com.cn/biotech/ OR https://manu60.magtech.com.cn/biotech/Y2006/V26/I03/26

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