[白细胞介素-6基因的克隆、表达及纯化]
[Interleukin-6 gene cloning, expression and purification].
作者信息
Ma X, Chen Z, Zheng H, Huang B, Cai L
机构信息
Institute of Basic Medical Sciences, CAMS and PUMC, Beijing 100005.
出版信息
Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 1998 Jun;20(3):185-90.
OBJECTIVE
The main purpose of this paper is to study the batch production of recombinant human interleukin-6(rhIL-6).
METHODS
The cloned rhIL-6 gene is under the control of T7 promoter of pET30a vector and expressed in E. coli.
RESULTS
The ratio of expressed recombinant protein to total cell protein is more than 50%. The rhIL-6 molecular weight is 21,000, isoelectric point is 6.7. The purity of the rhIL-6 is more than 95%, and the activity of rhIL-6, determined by IL-6 dependent mice hybridoma cell line 7TD1 and MTT assay, is 0.35 ng/ml.
CONCLUSIONS
All results mentioned show that rhIL-6 meets the request of the middle scale production.
目的
本文的主要目的是研究重组人白细胞介素-6（rhIL-6）的批量生产。
方法
克隆的rhIL-6基因受pET30a载体的T7启动子控制，并在大肠杆菌中表达。
结果
表达的重组蛋白与总细胞蛋白的比例超过50%。rhIL-6的分子量为21,000，等电点为6.7。rhIL-6的纯度超过95%，通过IL-6依赖的小鼠杂交瘤细胞系7TD1和MTT法测定，rhIL-6的活性为0.35 ng/ml。
结论
上述所有结果表明rhIL-6符合中规模生产的要求。
Zotero 插件