文献类型：期刊文献

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

作者：Yi, Lina; Yin, Xiaopu; Wei, Dongzhi; Ma, Yushu

机构：[1]E China Univ Sci & Technol, Inst Biochem, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2006

卷号：13

期号：8

起止页码：823

外文期刊名：PROTEIN AND PEPTIDE LETTERS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000239700600012)】；

语种：英文

外文关键词：exendin-4 dimer; recombinant expression; purification; chemical cross-linking

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.