Activity of purified hepatitis C virus protease NS3 on peptide substrates.

@article{Steinkhler1996ActivityOP,
  title={Activity of purified hepatitis C virus protease NS3 on peptide substrates.},
  author={Christian Steink{\"u}hler and Andrea Urbani and Licia Tomei and Gabriella Biasiol and Mohinder Sardana and Elisabetta Bianchi and Antonello Pessi and Raffaele De Francesco},
  journal={Journal of virology},
  year={1996},
  volume={70 10},
  pages={
          6694-700
        }
}
The protease domain of the hepatitis C virus (HCV) protein NS3 was expressed in Escherichia coli, purified to homogeneity, and shown to be active on peptides derived from the sequence of the NS4A-NS4B junction. Experiments were carried out to optimize protease activity. Buffer requirements included the presence of detergent, glycerol, and dithiothreitol, pH between 7.5 and 8.5, and low ionic strength. C- and N-terminal deletion experiments defined a peptide spanning from the P6 to the P4… CONTINUE READING
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