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�й�ҩѧ��־ 2009, Vol. 44 Issue (06) :411-414    DOI:
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1.���ľ�ҽ��ѧҩѧϵ ���� 710032;2.�������ݴ�ѧҽѧԺ ���������� ��ɼ� 90048
MA Xue1��HUI Hong-xiang2��ZHOU Ying1��HE Gong-hao1��MENG Jing-ru1��JIA Min1��LUO Xiao-xing1
1. School of Pharmacy��Fourth Military Medical University��Xi��an 710032��China; 2. Department of Medicine��University of California��California Los Angeles��CA 90048��USA

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ժҪ Ŀ�Ľ����������ȸ�Ѫ��������ǰҩ(prodrug of recom binant human GLPs,Pro-rhGLPs)�ı���������,�о�Pro-rhGLPs������Ѫ��ˮƽ��Ѫ���ȵ���ˮƽ��Ӱ�졣�������������-��-D-�����������(IPTG,0.01mmol��L-1)�յ�ԭ�˱��ϵͳE.coli BL21(DE3)/pET32a(+)-hGLPs���Pro-rhGLPs,12%SDS-PAGE��⵰�ױ����,Ni-NTA�׺Ͳ�������Pro-rhGLPs,Ӧ��Westernblot������۲�ǰ��ҩ��Ļ��Է����ͷŹ��̡���C57BL/6С���Ͻ�������������ʵ����������ѧ����,��ͬʱ����ȡѪ�ⶨѪ�Ǽ�Ѫ���ȵ���ˮƽ��������db/dbС���Ϲ۲��併�����á������������Pro-rhGLPsԭ�˱��ϵͳ��,Pro-rhGLPs�����ԼΪϸ���ܵ��׵�50%�������õ��ĵ��״��ȴﵽ95.43%,���ҿ�����������ø�����»�������,�ͷų�����ȸ�Ѫ��������1(GLP-1)���ӡ�������Pro-rhGLPs�ʼ��������Խ���Ѫ��Ũ��,ͬʱ����Ѫ���ȵ���ˮƽ���ȼ���Pro-rhGLPs�Ľ������ý�GLP-1���ø�ǿ�����۽�����Pro-rhGLPs��Ч����������,����˸ߴ���Pro-rhGLPs,������С��������ԵĽ�Ѫ�����á�
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Abstract�� OBJECTIVE To produce prodrug of recombinant human glucagon-like peptides (Pro-rhGLPs) and study its effects on regulations of blood glucose levels and insulin secretion in mice. METHODS The constructed E.coli BL21(DE3) /pET32a(+)-hGLPs was induced by 0.01 mmol��L-1 Isopropgl-��-D-thiogalactopyranoside(IPTG). The expressed product was identified by 12% SDS-PAGE. The protein was purified by Ni-NTA purification system. Pro-rhGLPs was digested by thrombin in PBS buffer. The biological activity of Pro-rhGLPs was examined by sc injection in C57BL/6 mice or db/db mice. Blood glucose levels were measured using a blood glucose meter. Plasma insulin concentrations were determined by ELISA. RESULTS The expression output of Pro-rhGLPs was approximately 50% of the total bacterial proteins. The purity of recombinant Pro-rhGLPs was more than 95.43% by HPLC analysis.The protein was slowly digested by specific endoproteinase and bioactive glucagons peptide 1(GLP-1) was released gradually. The analysis of in vivo activity indicated that Pro-rhGLPs had the bioactivity of native GLP-1,and significantly decreased blood glucose and increased insulin secretion in dose-dependent manner. Pro-rhGLPs had a stronger effects than GLP-1. Moreover,basal random glycemia decreased rapidly and remained lower level for 10 h following a single injection. CONCLUSION A prokaryotic expression system of Pro-rhGLPs with high efficiency was successfully established and the protein was obtained. Preliminary studies showed a new potential for developing the long-acting GLP-1 analogs for clinical applications.
Keywords�� diabetes,   human glucagons-like peptide l     
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.�������ȸ�Ѫ��������ǰҩ�ı�������������Է���[J]  �й�ҩѧ��־, 2009,V44(06): 411-414
.Expression,Purification and Bioactivity of Prodrug of Recombinant Human GLPs [J]  Chinese Pharmaceutical Journal, 2009,V44(06): 411-414
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