%0 Journal Article
%T Expression and Purification of Human Parathyroid Hormone Peptide ( 1-34 ) in Escherichia coli<br>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
%A LI Jian-feng
%A XIAO Hong-jian
%A JI Qiu-yan
%A LI Zhi-hua
%A LONG Hai-ting
%A YAN Ling-mei
%A LUO Na
%A XU Wei-ming
%A <br>李健峰
%A 肖红剑
%A 姬秋彦
%A 李智华
%A 龙海亭
%A 阎玲梅
%A 罗娜
%A 徐维明
%J 中国生物工程杂志
%D 2006
%I 
%X 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.
%K Human parathyroid hormone Escherichia coli Fusion expression<br>人甲状旁腺激素
%K 大肠杆菌
%K 融合表达
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=951380788B355DEA7D75520FA3B199C9&aid=592BAA4DC9E87659&yid=37904DC365DD7266&vid=96C778EE049EE47D&iid=38B194292C032A66&sid=96C778EE049EE47D&eid=340AC2BF8E7AB4FD&journal_id=1671-8135&journal_name=中国生物工程杂志&referenced_num=1&reference_num=7