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Separation of correctly refolded and mis-refolded consensus interferon by hydrophobic interaction chromatography / 生物工程学报
Chinese Journal of Biotechnology ; (12): 451-455, 2005.
Article in Chinese | WPRIM | ID: wpr-305252
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%.
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Protein Conformation / Recombinant Proteins / Interferon Type I / Chemistry / Chromatography, Liquid / Interferon-alpha / Protein Folding / Hydrophobic and Hydrophilic Interactions / Methods Language: Chinese Journal: Chinese Journal of Biotechnology Year: 2005 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Protein Conformation / Recombinant Proteins / Interferon Type I / Chemistry / Chromatography, Liquid / Interferon-alpha / Protein Folding / Hydrophobic and Hydrophilic Interactions / Methods Language: Chinese Journal: Chinese Journal of Biotechnology Year: 2005 Type: Article