Refolding and purification of recombinant human VEGF-121 expressed as inclusion bodies in Escherichia coli

VernacularTitle:大肠杆菌表达的人血管内皮细胞生长因子的复性与纯化研究
Author: Zhi-Ming HU ¹ ; Li MA ; Ming-Qian ZHOU ; Ji-Min GAO ; Xiao-Ning WANG
Author Information

1. 南方医科大学
Keywords: inclusion bodies; purification; refolding; vascular endothelial growth factor
From: Journal of Southern Medical University 2006;26(8):1083-1086
CountryChina
Language:Chinese
Abstract: Vascular endothelial growth factor 121 (VEGF121) was expressed as inclusion bodies by recombinant Escherichia coli. High concentrations of both biomass (46 g dry cell/L) and VEGF121 inclusion bodies (4.5 g/L) were obtained by applying a high-cell-density culture. After the inclusion bodies were washed and dissolved, VEGF121 was refolded at 0.2 mg/ml by ultrafiltration in refolding buffer with a yield of 81%. Renatured VEGF121 was purified by anion chromatography and Sephacry S-100 chromatography with purity higher than 95% and fnal purification yield of 31%. The purified VEGF121 could stimulate the proliferation of human umbilical vein endothelial cells as demonstrated by a biological activity assay.