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Tuyển tập các báo cáo nghiên cứu khoa học ngành y học tạp chí Medical Sciences dành cho các bạn sinh viên ngành y tham khảo đề tài: Expression of Human Globular Adiponectin-Glucagon-Like Peptide-1 Analog Fusion Protein and Its Assay of Glucose-Lowering Effect In Vivo. | Int. J. Med. Sci. 2011 8 203 International Journal of Medical Sciences 2011 8 3 203-209 Research Paper Expression of Human Globular Adiponectin-Glucagon-Like Peptide-1 Analog Fusion Protein and Its Assay of Glucose-Lowering Effect In Vivo Tongfeng ZhaolX Jing Lv1 Jiangpei Zhao2 Xiao Huang3 and Haijuan Xiao1 1. Department of Geriatrics the Second Affiliated Hospital School of Medicine Zhejiang University Hangzhou 310000 PR China 2. Department of Geriatrics Hangzhou Hospital of Traditional Chinese Medicine Hangzhou 310000 PR China 3. College of Life Sciences Zhejiang University Hangzhou 310000 PR China H Corresponding author Tongfeng Zhao Ph.D. Department of Geriatrics the Second Affiliated Hospital School of Medicine Zhejiang University Hangzhou 310000 PR China. Tel 86-571-887783690 Fax 86-571-87022660 e-mail zhaotongfeng@yahoo. com.cn Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License http creativecommons.org licenses by-nc-nd 3.0 . Reproduction is permitted for personal noncommercial use provided that the article is in whole unmodified and properly cited. Received 2010.11.17 Accepted 2011.03.01 Published 2011.03.04 Abstract In this study human globular adiponectin-glucagon-like peptide-1 analog gAd-GLP-1-A fusion protein was expressed and its glucose-lowering effect was measured in vivo. We constructed a prokaryotic expression vector PET28a-gAd-GLP-1-A and transformed the vector into Escherichia coli BL21 DE3 . A recombinant fusion protein of about 25KD was expressed from BL21 DE3 cells after isopropylthio-P-D-galactoside induction. This protein was N-terminal His-tagged gAd-GLP- 1 -A fusion protein. Most of the protein was expressed in inclusion body. The fusion protein in inclusion body was purified by using High-Affinity Nickel Iminodiacetic Acid Resin and refolded in urea gradient refolding buffer. The refolded protein was incubated with enterokinase to remove the N-terminal His-tag. .
