Expression, Renaturation and Simultaneous Purification of Recombinant Human Stem Cell Factor in Escherichia coli

被引：0
|
作者：
Wang Lili
Wang Chaozhan
Geng Xindu
机构：
[1] Northwest University,Institute of Modern Separation Science, Key Lab of Modern Separation Science in Shaanxi Province
来源：
Biotechnology Letters | 2006年 / 28卷
关键词：
High performance hydrophobic interaction chromatography; Inclusion bodies; Protein purification; Protein refolding; Recombinant human stem cell factor;
D O I：
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中图分类号：
学科分类号：
摘要：
Recombinant human stem cell factor (rhSCF) was produced as an inclusion body by Escherichia coli DH5α grown in a 5 l fermentor. Inclusion bodies of rhSCF were purified and solubilized in urea solution, then renatured with simultaneous purification using a high performance hydrophobic interaction chromatographic (HPHIC) squat column. The refolded rhSCF had a purity of 94% and a bioactivity of 1.2 × 106 IU mg−1of rhSCF protein. The method described is fast and simple to implement.
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页码：993 / 997
页数：4
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