%0 Journal Article
%T Purification and Characterization of Glucagon-Like Peptide-1 and Human Serum Albumin Fusion Protein Expressed in Pichia pastoris<br>重组胰高血糖素样肽-1与人血清白蛋白融合蛋白的纯化及活性研究
%A CHEN Jia-Qi
%A GAO Zhi-Hui
%A ZHU Yuan-Yuan
%A YANG Wen-Bo
%A BAI Gang
%A <br>陈家琪
%A 高智慧
%A 朱元元
%A 杨文博
%A 白钢
%J 微生物学报
%D 2007
%I 
%X A fusion protein of glucagons-like peptide-1 and human serum albumin (GLP-1/HSA) was expressed and secreted into the fermentation broth with recombinant Pichia pastoris. The productivity of expressed GLP-1/HSA could reach 63.6mg/L in 10L fermentor. After concentrated with hollow-fiber ultrafiltration membrane, GLP-1/HSA was purified from fermentation broth by hydrophobic chromatography, negative ion exchange chromatography and gel filtration chromatography in turn. The HPLC analysis showed that the purified GLP-1/HSA had an overall purity of 95.8%. Furthermore, the analysis of in vivo activity indicated that GLP-1/HSA had the bioactivity of native GLP-1, and could significantly reduce blood glucose level 4h after intraperitoneal administration. It was concluded that a great deal of GLP-1/HSA with higher purity could be harvested by Pichia pastoris expression system and the established purification methods. Preliminary studies show a new potential for developing the long-acting GLP-1 analogs for clinical applications.
%K Glucagon-like peptide-1
%K Human serum albumin
%K Fusion expression
%K Purification<br>胰高血糖素样肽-1，人血清白蛋白，融合表达，纯化
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=C8030789A4F94A3EFDC2EAA4C54DFCA6&yid=A732AF04DDA03BB3&vid=339D79302DF62549&iid=94C357A881DFC066&sid=8FAB510F8256A102&eid=78665150E17BD102&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=0