【题名】：Intein-mediated expression and purification of an analog of glucagon-like peptide-1 in Escherichia coli.
【作者】：Ma C, Gao M, Liu W, Zhu J, Tian H, Gao X, Yao W.
【杂志名全称】：Protein Pept Lett
【年, 卷(期), 起止页码】：2010 Oct;17(10):1245-50.
【全文链接】：
http://www.ncbi.nlm.nih.gov/pubmed/20441562【摘要信息】：To facilitate expression and purification of an analog of GLP-1 (mGLP-1), an intein system was employed in this study. A recombinant fusion protein, CBD-DnaB-mGLP-1, was constructed and expressed in the form of inclusion body. After refolding, the intein-mediated self-cleavage was triggered by pH and temperature shift. By using chitin beads column followed by single step purification, about 2.58 mg of mGLP-1 with the purity of up to 98% could be obtained from 1 L medium. Tricine-SDS-PAGE, RP-HPLC, and ESI-MS were undertaken to determine the purity and molecular weight of mGLP-1. The glucose-lowering activity of mGLP-1 was also preliminarily determined.
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