Separation of correctly refolded and mis-refolded consensus interferon by hydrophobic interaction chromatography.
- Author:
Rong-Zhi ZHAO
1
;
Yong-Dong LIU
;
Fang-Wei WANG
;
Jing-Jing LI
;
Xin XIA
;
Zhi-Guo SU
Author Information
1. Civil & Environmental Engineering School, University of Science and Technology of Beijing, Beijing 100083, China.
- Publication Type:Journal Article
- MeSH:
Chromatography, Liquid;
methods;
Hydrophobic and Hydrophilic Interactions;
Interferon Type I;
chemistry;
isolation & purification;
Interferon-alpha;
Protein Conformation;
Protein Folding;
Recombinant Proteins
- From:
Chinese Journal of Biotechnology
2005;21(3):451-455
- CountryChina
- Language:Chinese
-
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%.
