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Updated: Aug 16, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
[Separation of correctly refolded and mis-refolded consensus interferon by hydrophobic interaction chromatography]
Rong-Zhi Zhao1, Yong-Dong Liu, Fang-Wei Wang
1Civil & Environmental Engineering School, University of Science and Technology of Beijing, Beijing 100083, China.
Abstract:
Hydrophobic interaction chromatography was used to separate correctly refolded and mis-refolded consensus interferon. The effects of ligand types, salt concentration, pH and flow rate were investigated. The best result could be obtained by using Butyl Sepharose 4 Fast Flow, 0.8 mol/L of ammonium sulfate, pH 8.3 and 90cm/h of linear flow rate. Reverse-phase HPLC analysis showed the purity of the pooled fraction was as high as 99.6%. The specific activity of purified consensus interferon was 2.3 x 10(9) IU/mg, The mass recovery of targeth protein was 36.7%.
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