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Effect of N-terminal solubility enhancing fusion proteins on yield of purified target protein

Journal article
Authors M. Hammarstrom
E. A. Woestenenk
N. Hellgren
H. Berglund
Torleif Härd
Published in Journal of structural and functional genomics
Volume 7
Issue 1
Pages 1-14
ISSN 1345-711X (Print)
Publication year 2006
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 1-14
Language en
Keywords Chromatography, Affinity/methods, *Escherichia coli/genetics, *Gene Expression, Humans, Recombinant Fusion Proteins/biosynthesis/genetics/*isolation &, purification, Solubility
Subject categories Medical cell biology


We have studied the effect of solubilising N-terminal fusion proteins on the yield of target protein after removal of the fusion partner and subsequent purification using immobilised metal ion affinity chromatography. We compared the yield of 45 human proteins produced from four different expression vectors: three having an N-terminal solubilising fusion protein (the GB1-domain, thioredoxin, or glutathione S-transferase) followed by a protease cleavage site and a His tag, and one vector having only an N-terminal His tag. We have previously observed a positive effect on solubility for proteins produced as fusion proteins compared to proteins produced with only a His tag in Escherichia coli. We find this effect to be less pronounced when we compare the yields of purified target protein after removal of the solubilising fusion although large target-dependent variations are seen. On average, the GB1+His fusion gives significantly higher final yields of protein than the thioredoxin+His fusion or the His tag, whereas GST+His gives lower yields. We also note a strong correlation between solubility and target protein size, and a correlation between solubility and the presence of peptide fragments that are predicted to be natively disordered.

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