Purification and characterization of recombinant murine endostatin in E. coli
Endostatin, a carboxyl-terminal fragment of collagen XVIII is known as an anti-angiogenic agent, that specifically inhibits the proliferation of endothelial cell and the growth of several primary tumor. We report here the purification and characterization of the recombinant murine endostatin (rmEndo...
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Veröffentlicht in: | Experimental & molecular medicine 1999-12, Vol.31 (4), p.197-202 |
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creator | You, W K So, S H Lee, H Park, S Y Yoon, M R Chang, S I Kim, H K Joe, Y A Hong, Y K Chung, S I |
description | Endostatin, a carboxyl-terminal fragment of collagen XVIII is known as an anti-angiogenic agent, that specifically inhibits the proliferation of endothelial cell and the growth of several primary tumor. We report here the purification and characterization of the recombinant murine endostatin (rmEndostatin) which was expressed in a prokaryotic expression system. This rmEndostatin has similar physiochemical properties of yeast-produced recombinant endostatin, and it also specifically inhibits the proliferation and migration of bovine capillary endothelial cells stimulated by basic fibroblast growth factor. The biological activity of rmEndostatin was also shown by its anti-angiogenic ability on the chorioallantoic membrane of chick embryo in vivo. In this article, we demonstrate the refolding and purification of rmEndostatin, expressed using E. coli system, to a biologically active and soluble form. In addition, these results confirm the activity of endostatin as a potent anti-angiogenic agent. |
doi_str_mv | 10.1038/emm.1999.32 |
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We report here the purification and characterization of the recombinant murine endostatin (rmEndostatin) which was expressed in a prokaryotic expression system. This rmEndostatin has similar physiochemical properties of yeast-produced recombinant endostatin, and it also specifically inhibits the proliferation and migration of bovine capillary endothelial cells stimulated by basic fibroblast growth factor. The biological activity of rmEndostatin was also shown by its anti-angiogenic ability on the chorioallantoic membrane of chick embryo in vivo. In this article, we demonstrate the refolding and purification of rmEndostatin, expressed using E. coli system, to a biologically active and soluble form. In addition, these results confirm the activity of endostatin as a potent anti-angiogenic agent.</abstract><cop>United States</cop><pmid>10630374</pmid><doi>10.1038/emm.1999.32</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Angiogenesis Inhibitors - genetics Angiogenesis Inhibitors - isolation & purification Angiogenesis Inhibitors - pharmacology Animals Blotting, Western Cattle Cell Movement - drug effects Chick Embryo Chorion - drug effects Chorion - pathology Circular Dichroism Collagen - genetics Collagen - isolation & purification Collagen - pharmacology Collagen Type XVIII Electrophoresis, Polyacrylamide Gel Endostatins Endothelium, Vascular - cytology Endothelium, Vascular - drug effects Escherichia coli - genetics Fibroblast Growth Factor 2 - pharmacology Mice Neovascularization, Physiologic - drug effects Peptide Fragments - genetics Peptide Fragments - isolation & purification Peptide Fragments - pharmacology Protein Folding Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - pharmacology Solubility Yeasts - genetics |
title | Purification and characterization of recombinant murine endostatin in E. coli |
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