Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8360130 | Protein Expression and Purification | 2015 | 7 Pages |
Abstract
A purification scheme based on hydrophobic interaction chromatography was developed to separate inactivated foot-and-mouth disease virus (FMDV) from crude supernatant. About 92% recovery and 8.8-fold purification were achieved on Butyl Sepharose 4FF. Further purification on Superdex 200 resulted in another 29-fold purification, with 92% recovery. The columns were coupled through an intermediate ultrafiltration unit to concentrate the virus. The entire process was completed in about 3.5Â h, with 75% final FMDV recovery, and 247-fold purification. The final product had purity above 98%, with over 99.5% of host cell DNA removed. High-performance size exclusion chromatography (HPSEC), Western blot, dynamic light scattering (DLS), and transmission electron microscopy (TEM) indicated that the purified virus contained the required antigen, and was structurally intact with a spherical shape and a particle size of 28Â nm.
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Authors
Hao Li, Yanli Yang, Yan Zhang, Songping Zhang, Qizu Zhao, Yuanyuan Zhu, Xingqi Zou, Mengran Yu, Guanghui Ma, Zhiguo Su,