摘要
Lon蛋白酶是一种在各种生物体内广泛分布并且具有多种生物功能的蛋白质.以嗜热栖热菌(Thermus thermophilus HB8)的Lon蛋白酶(TTLon)为研究对象,将TTLon蛋白酶的编码基因克隆至pTrc His载体,并在大肠杆菌中进行了成功表达,采用Ni-NTA亲和层析对其进行分离纯化,并通过一系列实验证明Lon蛋白酶能够与ATP结合,具有依赖ATP的蛋白酶活性和依赖ATP的分子伴侣活性.
Lon proteases are conserved in all living organisms and play important biological roles.With the material of Lon protease from Thermus thermophilus HB8,the gene was cloned and connected to the plasmid pTrcHis.TTLon protease was successfully expressed in E.coli.The recombinant protein was purified with affinity chromatography(Ni-NTA).A series of experiments showed that the TTLon can bind with ATP,the activity of protease and the activity of molecular chaperone were both ATP-dependent.
出处
《首都师范大学学报(自然科学版)》
2009年第5期35-39,53,共6页
Journal of Capital Normal University:Natural Science Edition
基金
国家自然科学基金资助(Nr.30870053)