Protein solubility and differential proteomic profiling of recombinant <Emphasis Type="Italic">Escherichia coli</Emphasis> overexpressing double-tagged fusion proteins |
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| Authors: | Chung-Hsien Cheng Wen-Chien Lee |
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| Institution: | (1) Department of Chemical Engineering, Systems Biology and Tissue Engineering Research Center, National Chung Cheng University, 621 Chiayi, Taiwan |
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| Abstract: | Background Overexpression of recombinant proteins usually triggers the induction of heat shock proteins that regulate aggregation and
solubility of the overexpressed protein. The two-dimensional gel electrophoresis (2-DE)-mass spectrometry approach was used
to profile the proteome of Escherichia
coli overexpressing N-acetyl-D-glucosamine 2-epimerase (GlcNAc 2-epimerase) and N -acetyl-D-neuraminic acid aldolase (Neu5Ac aldolase), both fused to glutathione S-transferase (GST) and polyionic peptide
(5D or 5R). |
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