Expression and purification of exendin-4, a GLP-1 receptor agonist, in Escherichia coli

被引：20

作者：

Yin, XP ^{[1
]}

Wei, DZ ^{[1
]}

Yi, LN ^{[1
]}

Tao, XY ^{[1
]}

Ma, YS ^{[1
]}

机构：

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

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2005年 / 41卷 / 02期

基金：

国家高技术研究发展计划(863计划);

关键词：

exendin-4; expression; glucose-lowering action;

D O I：

10.1016/j.pep.2004.10.014

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Exendin-4 is a 39 amino acid peptide isolated from salivary secretions of Gila monster (Heloderma suspectrum). It shows 53% sequence similarity to glucagon-like peptide-1 (GLP-1), which is evaluated for the regulation of plasma glucose in type 2 diabetes. Exendin-4 is a potent and long-acting agonist of GLP-1 receptor. In the present Study, the exendin-4 gene obtained by PCR with an enterokinase site at N-terminus and a termination codon at C-terminus was expressed in Escherichia coli strain BL21 (DE3) harboring pET32a(+). The fusion protein was purified by chromatography on Ni-NTA-agarose column. Recombinant exendin-4 was obtained by enterokinase cleavage of the fusion protein and subsequent purification. The yield of recombinant exendin-4 was 3.15 mg/10g bacteria. The obtained recombinant exendin-4 shows glucose-lowering action in vivo. (c) 2004 Elsevier Inc. All rights reserved.

引用

页码：259 / 265

页数：7