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合成亮氨酸脑啡肽基因在大肠杆菌中的克隆与表达。

The cloning and expression of the synthetic leu-enkephalin gene in E. coli.

作者信息

Ao S Z, Liang Z H, Tang J Y, Zhou X X, Ding X H, Chen C Q, Li Z P

出版信息

Sci Sin B. 1984 Jan;27(1):28-36.

PMID:6374891
Abstract

The synthetic leu-enkephalin (LEK) gene was joined with pBR322 and transformed to E. coli. The recombinant plasmids containing the LEK gene were selected by colony hybridization, and characterized by restriction mapping and Southern's technique. The lac operon was used to control the expression of the LEK gene. A recombinant plasmid, pEL 103, in which the lac operon and LEK gene are transcribed in the same direction, produces LEK in E. coli. The level of LEK detected by radioimmunoassay reaches 426 ng per mg of bacterial protein.

摘要

将合成的亮氨酸脑啡肽(LEK)基因与pBR322连接,并转化到大肠杆菌中。通过菌落杂交筛选出含有LEK基因的重组质粒,并用限制性酶切图谱和Southern技术进行鉴定。利用乳糖操纵子控制LEK基因的表达。一种重组质粒pEL 103,其中乳糖操纵子和LEK基因同向转录,可在大肠杆菌中产生LEK。通过放射免疫测定法检测到的LEK水平达到每毫克细菌蛋白426纳克。

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