单环刺螠纤溶酶ufeII基因的原核表达及活性研究  

Prokaryotic expression and activity of fibrinolytic enzyme ufeIIfromUrechis unicinctus

作　　者：孙雪燕[1] 宋鸿旭 任宇豪 梁鹏宇[1] 律倩倩 刘伟治[1] 

机构地区：[1]中国海洋大学海洋生命学院,山东青岛266003

出　　处：《中国科技论文》2016年第24期2797-2800,2815,共5页China Sciencepaper

基　　金：高等学校博士学科点专项科研基金资助项目(20130132120031);国家自然科学基金资助项目(81302684);山东省自然科学基金资助项目(ZR2013CM044)

摘　　要：血栓类疾病的治疗已成为当今医学界研究的重点、难点问题之一。单环刺螠纤溶酶UFEII是从海洋生物单环刺螠体内分离纯化出的具有纤溶活性的丝氨酸蛋白酶。通过基因工程技术对ufeII基因构建了单环刺螠纤溶酶UFEII的体外重组表达系统,通过包涵体复性获得了具有纤溶活性的重组UFEII,并对其体外活性进行了研究。通过纤维平板法说明重组UFEII具有水解血纤维蛋白的能力,并且血纤维蛋白原降解实验显示其对血纤维蛋白原的降解顺序是优先降解α链,其次是β链、γ链。研究结果表明,重组UFEII是1种有潜力的新型溶栓剂。Treatment of thrombotic diseases has become one of the key and difficult issues in today＇s medical research.Fibrinolytic enzyme UFEII is the serine protease with high fibrinolytic activity,which is extracted and purified from marine invertebrate Urechis unicinctus.The recombinant prokaryotic expression UFEII was constructed,and the recombinant UFEII protein was obtained by refolding from the inclusion bodies.Furthermore,the enzymatic activity was characterized in vitro as well.The Fibrin plates assay demonstrates that the recombinant UFEII is capable of dissolving the fibrin.And the fibrinogen cleavage pattern assay shows that the recombinant UFEII has the cleavage preference for the chainα,and then chainβ,γ.These results indicate that recombinant UFEII is a promising novel thrombolytic agent.

关 键 词：酶学 单环刺螠纤溶酶 原核表达 活性 

分 类 号：Q55[生物学—生物化学] Q78