Core, NS3 and NS4 regions of Korean type hepatitis C virus(HCV) genome were expressed and purified as the form of fusion proteins by using a prokaryotic expression-purification system. Core protein, which was expressed up to 20% of total proteins
as a
-galactosidase fusion protein in E. coli, was purified by cleavage with cyanogen bromide(CNBr) followed by cation exchange chromatography. Nonstructural proteins, which were up to 25% of total proteins as a soluble maltose binding protein(MBP)
fusion
protein in E. coli, were purified by affinity chromatography, factor Xa cleavage and gel filtration. The purified Core(CP14), NS3(P27) and NS4(P14) proteins, which were confirmed as a single band of approximate 14Kda, 27Kda and 14Kda respectively
by
SDS-polyacrylamide gel electrophoresis, showed the strong immunoreactivity with antibodies in sera of Korean chronic hepatitis C patients on immunoblotting analysis.
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