摘要
利用实验室保存的重组质粒pMD18-MSTN重新构建原核表达质粒pET-32a-MSTN,将其转化到宿主菌大肠杆菌BL21上并进行诱导表达,再将所表达的融合蛋白进行纯化。结果表明:该基因在宿主菌中成功表达;目的蛋白被成功纯化,且纯度较高。
The recombinant plasmid pET- 32a- MSTN was eonstructed aeeording to the plasmid pMD18 -MSTN preserved in our laboratory and then was transformed into BL21 to express target protein. The result showed that the gene ean be expressed in E. eoli. The expressed produet was purified. Therefor the target protein can be purified and the purity was on a high level.
出处
《黑龙江畜牧兽医》
CAS
北大核心
2008年第7期18-20,共3页
Heilongjiang Animal Science And veterinary Medicine
基金
国家自然科学基金项目(30571341)
关键词
南海黄鸡
肌抑素基因
原核表达
蛋白纯化
Nanhai yellow ehieken
myostatin
prokaryotie expression
protein purifieation