摘要
本文从哥伦比亚生态型的拟南芥(Arabidopsis thaliana Columbia 0)中克隆了谷胱甘肽过氧化物酶AtGPX3的完整编码序列(Coding sequence,CDS)以及部分片段的CDS序列,构建了该基因的不同区域的表达载体,在Transetta(DE3)的BL21大肠杆菌中表达,并成功纯化了GPX3膜蛋白,不仅为后续实验研究GPX3的结构与功能提供了材料,而且为研究膜蛋白表达与纯化的方法提供了借鉴.
In this study, the author cloned the whole coding sequence and some fragments of GPX3 from Arabidopsis thaliana ecotype Columbia, and constructed them to some expression vectors, and then transformed the vectors into Escherichia coli strain Rosetta （DE3） and the GPX3 was purified successfully. The work not only provides materials for the further study of the structure and function of the GPX3, but also offers a method for expressing and purifying the membrane proteins.
出处
《河南大学学报（自然科学版）》
CAS
北大核心
2013年第6期662-666,共5页
Journal of Henan University:Natural Science
基金
国家自然科学基金资助项目(30770170)
关键词
原核表达
纯化
谷胱甘肽过氧化物酶
拟南芥
prokaryotic expression
purification
glutathione peroxidase
ArabidoI）sis thaliana
