%0 Journal Article
%T Purification of the Recombinant Fusion Protein Staphylokinase-Hirudin Expressed in Escherichia cloi and its Analysis of Self-association in Solution<br>大肠杆菌表达的重组葡激酶-水蛭素融合蛋白的分离纯化及其二聚体分析
%A ZHONG Gen-shen
%A YU Ai-ping
%A JIN Ji-de
%A JIANG Zhong-hua
%A WU Zu-ze
%A <br>钟根深
%A 于爱平
%A 靳继德
%A 蒋中华
%A 吴祖泽
%J 中国生物工程杂志
%D 2007
%I 
%X The recombinant fusion protein staphylokinase-hirudin(rSFH) was purified from the high density-fermented engineered E.coli by means of ion-exchange chromatography (IEC) and gel filtration (GF). The purity of rSFH reached to more than 98% determined by RP-HPLC and SDS-PAGE, and the yield was up to 0.7g per liter of fermentation broth. The analysis of homologous dimmer of rSFH appeared during the purification and calculation of the surface hydrophobic area had been carried out by means of hydrophobic chromatography and MALD-TOF. The influence of sodium chloride and temperature on the behavior of rSFH reversible dimerization was analyzed by high performance sized- exclusive chromatography(HPSEC). It is concluded that the hydrophobic interaction played an important role in the reversible dimerization of rSFH.
%K Staphylokinase Hirudin rSFH Purification Dimerization<br>葡激酶
%K 水蛭素
%K 纯化
%K 二聚体
%K 疏水作用
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=951380788B355DEA7D75520FA3B199C9&aid=A2125DBBE6621F07&yid=A732AF04DDA03BB3&vid=DB817633AA4F79B9&iid=0B39A22176CE99FB&sid=6209D9E8050195F5&eid=ECE8E54D6034F642&journal_id=1671-8135&journal_name=中国生物工程杂志&referenced_num=0&reference_num=28