Expression and purification of exendin-4 dimer in Escherichia coli and its interaction with GLP-1 receptor in vitro

被引：6
|
作者：
Yi, Lina [1 ]
Yin, Xiaopu [1 ]
Wei, Dongzhi [1 ]
Ma, Yushu [1 ]
机构：
[1] E China Univ Sci & Technol, Inst Biochem, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China
来源：
PROTEIN AND PEPTIDE LETTERS | 2006年 / 13卷 / 08期
关键词：
exendin-4; dimer; recombinant expression; purification; chemical cross-linking;
D O I：
10.2174/092986606777841226
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Exendin-4 is a 39 amino acid peptide isolated from the Gila monster salivary gland. It is 53% homologous to GLP-1 and exhibits similar glucoregulatory activities. In this study, exendin-4 dimer (D-Ex4) was constructed, cloned into plasmid pET32a(+) and expressed in E. coli BL21(DE3). The fusion protein with His-tag at the N-terminus was purified with a Ni-NTA-agarose column. After proteolytic cleavage, D-Ex4 peptide with high purity was obtained by HPLC. The results obtained by chemical cross-linking showed that D-Ex4 maintained affinity to GLP-1 receptor.
引用
收藏
页码：823 / 827
页数：5
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