Xing-Wen Yang

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To investigate the role of C-peptide in the folding of insulin precursor, a series of C-peptide mutant proinsulin genes were constructed, overexpressed in Escherichia coli and the proteins purified. Correct disulfide linkages of these proteins were confirmed by both tryptic peptide mapping and insulin receptor binding analyses. In vitro refolding(More)
Protein engineering techniques were employed to graft the known anticoagulant Arg-Gly-Asp (RGD) motif-containing sequences onto the surface of a mutant, inactive insulin framework. To probe the effect of a disulfide bond on the resultant anticoagulant activity, a native RGD-containing sequence from disintegrin dendroaspin, CFTPRGDMPGPYC, as well as a(More)
A naked plasmid with human pre-pro-insulin gene was transferred into skeletal muscle of diabetic rats by electric pulses and gene expression was detected. Blood glucose concentration was decreased from 24 mmol l−1 to 8.5 mmol l−1. Circulating insulin-like protein was increased significantly to 15–20 μU ml−1, while that of the control group injected with the(More)
The cDNA gene encoding human prorelaxin H2 was subcloned from plasmid pMAL p2X-hRLX H2 into the EcoRI and BamHI sites of prokaryotic expression vector pBV220, resulting in the recombinant plasmid pBV220-hPRLX H2, which was subsequently transformed into Escherichia coli DH5arg;. The target gene was highly expressed in the form of inclusion body by(More)
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