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Solubilization and refolding with simultaneous Purification
of Recombinant Human Granulocyte Colony-stimulating
Factor expressed by Escherichia coli as Inclusion Bodies1
Wang Chaozhan ，Wang Lili ，Geng Xindu
Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of
Education ，Institute of Modern Separation Science ，Key Laboratory of Separation Science in
Shaanxi Province, Department of Chemistry，Northwest University ，Xi’an （710069 ）
E-mail ：czwang@
Abstract
Recombinant human granulocyte colony-stimulating factor (rhG-CSF) was solubilized and purified
from inclusion bodies expressed in Escherichia coli . Effect of both pH and urea on the
solubilization of rhG-CSF inclusion bodies were investigated, the results indicate that the existence
both ionic and hydrophobic interactions in the inclusion bodies. Various solvents with
reduced/oxidized glutathione (GSH/GSSG) were used to solubilize rhG-CSF inclusion bodies ，the
extent of solubilization was compared with each other and the behaviors of rhG-CSF in high
performance hydrophobic interaction chromatography (HPHIC) were investigated. Solubilization
of rhG-CSF inclusion bodies by 2% Sarkosyl in the presence of GSH/GSSG probably helps
oxidizing rhG-CSF to form disulfide bonds, but Sarkosyl in the solution interferes seriously with
the chromatographic process. To solubilize rhG-CSF inclusion bodies by combination of 2%
Sarkosyl and 8.0 mol⋅L-1 urea can overcome this problem very well. And the so solubilized
rhG-CSF was simultaneously refolded and purified by one s
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