重组人干细胞因子在大肠杆菌中的表达、复性及同步纯化
Expression, renaturation and simultaneous purification of recombinant human stem cell factor in Escherichia coli.
作者信息
Lili Wang, Chaozhan Wang, Xindu Geng
机构信息
Institute of Modern Separation Science, Key Lab of Modern Separation Science in Shaanxi Province, Northwest University, Xi'an 710069, China.
出版信息
Biotechnol Lett. 2006 Jul;28(13):993-7. doi: 10.1007/s10529-006-9032-8. Epub 2006 Jun 20.
Recombinant human stem cell factor (rhSCF) was produced as an inclusion body by Escherichia coli DH5alpha 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 x 10(6 )IU mg(-1)of rhSCF protein. The method described is fast and simple to implement.
重组人干细胞因子（rhSCF）由在5升发酵罐中培养的大肠杆菌DH5α作为包涵体产生。rhSCF的包涵体经纯化后在尿素溶液中溶解，然后使用高效疏水相互作用色谱（HPHIC）短柱在复性的同时进行纯化。复性后的rhSCF纯度为94%，生物活性为1.2×10⁶ IU mg⁻¹ rhSCF蛋白。所述方法实施起来快速且简单。
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