Articles
Refolding Recombinant Human Granulocyte Colony Stimulating Granulocyte Colony Stimulating
February 17, 2009
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•Feature Article: Refolding Recombinant Human Granulocyte Colony Stimulating Factor Expressed By E. coli
•Feature Article: Refolding Recombinant Human Granulocyte Colony Stimulating Factor Expressed By E. coli
•Feature Article: Refolding Recombinant Human Granulocyte Colony Stimulating Factor Expressed By E. coli
By Chaozhan Wang, Lili Wang, and Xindu Geng
Refolding of recombinant proteins expressed in Escherichia coli is known as a bottleneck in their production and product manufacturing. Refolding yields are often low using traditional methods such as dialysis, dilution, or diafiltration. Liquid chromatography (LC) has recently been applied to protein refolding to increase yields (1, 2). In the 1990s, one of us first presented the refolding of rhIFN-? by high-performance hydrophobicinteraction chromatography (HPHIC) (3), with its bioactivity two- to threefold better than that of a dilution method, and obtained a patent based on this method (4). Since then, HPHIC has been applied to the refolding of many proteins. Click Here To Download:•Feature Article: Refolding Recombinant Human Granulocyte Colony Stimulating Factor Expressed By E. coli
