作　　者： ; ; ; ; ;

机构地区： 华南理工大学生物科学与工程学院

出　　处： 《华南理工大学学报（自然科学版）》 2005年第10期90-92,共3页

摘　　要： 通过分析降血压肽结构与功能的关系,设计并合成5条降血压肽序列.通过活性测定以及体外消化试验,确定P3(六肽)为理想降血压肽.为实现该小肽在大肠杆菌中的表达,经特定酶切位点将其串联为6拷贝的融合多肽,将相应的基因序列克隆至表达载体pGEX-4T-2并转化至宿主菌Escherichia coli BL21中.双酶切、PCR以及测序结果均表明成功构建了重组质粒pGEX-4T-2-ACEIP. Five angiotensin-converting enzyme inhibitor peptide （ACEIP） sequences were first designed and synthesized according to the relationship between the function and the structure of ACEIP. Next, the optimal peptide, namely, P3 （six-amino-acid sequence） was determined by the bioactivity measurement and the digesting test in vitro. It was then jointed at the specific enzyme cleavage site to construct a six-copy fusion peptide. The corresponding coding gene was cloned into pGEX-4T-2. The fusion expression vector of pGEX-4T-2-ACEIP was finally transformed into Escherichia coli BL21. The results of the double enzyme-cleavage, PCR and the sequence analysis all indicate that the recombinant plasmid pGEX-4T-2-ACEIP is successfully constructed.

关 键 词： 降血压肽 序列设计 基因重组

领　　域： [生物学]