Abstract
Both the NS3 protease and the NS4A protein are required for efficient cleavage of the nonstructural protein region of the hepatitis C virus polyprotein. The NS3 protease domain was fused at its C-terminal end with full length NS4A and expressed inEscherichia coli.This protein (NS3Δ-NS4A) was purified to apparent homogeneity after refolding from extracts recovered from inclusion bodies. During the expression and purification process, NS3Δ-NS4A was not auto-processed in either acisortransmanner at NS3/NS4A junction site. When thekcat/Kmvalues and thermostability of NS3Δ-NS4A were compared with those for maltose binding protein-NS3 fusion protein (MBP-NS3), which contains only NS3 region, the single-chain NS3Δ-NS4A showed enhanced proteolytic activities and thermostability.
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