Title: Prokaryotic expression, refolding, and purification of functional human vascular endothelial growth factor isoform 165: Purification procedures and refolding conditions revisited
Authors: Lee, I-Liang
Li, Pei-Shan
Yu, Wei-Lin
Shen, Hsin-Hsin
Department of Biological Science and Technology
Keywords: Expression;Purification;Refolding;Recombinant VEGF protein;Angiogenesis;Untagged protein
Issue Date: 1-Mar-2011
Abstract: Human vascular endothelial growth factor isoform 165 (VEGF165) is the first known member belonging to the VEGF protein family that plays a critical role in new blood vessel formation in vivo. This study presents a new protocol with optimized conditions for rapidly producing untagged recombinant and biological active human VEGF165 (rhVEGF165) using Escherichia coli cells. Protein was isolated from inclusion bodies, purified by gel filtration and ion exchange chromatography, and subjected to protein refolding and renaturation. The biological activity of rhVEGF165 is comparable with VEFG from eukaryotic source according to human umbilical vein endothelial cells (HUVEC) proliferation assay. Therefore, the present procedures provide a fast and easy way to produce this therapeutic protein. (C) 2010 Published by Elsevier Inc.
URI: http://dx.doi.org/10.1016/j.pep.2010.08.014
ISSN: 1046-5928
DOI: 10.1016/j.pep.2010.08.014
Volume: 76
Issue: 1
Begin Page: 54
End Page: 58
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