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文献和实验Expression and Purification of Hepatitis C Virus Protease from Clinical Samples
This chapter describes the procedures for production of recombinant hepatitis C virus (HCV) NS3 protease from clinical samples, which can be used in the biochemical assays to assess the impact of different drug-resistant mutations in the NS
has been purified and characterized (3 ,6 –8 ). The enzyme is a 204-residue monomer of 24,838 Dalton with a pI of 10.59 and optimal activity at 45�C and pH 8.0. The recombinant enzyme is stimulated by an 11-amino acid cleavage fragment from viral protein pre-VI
with 4 cm3 buffer and 1 cm3 of fruit extract). Read the absorbance and note the time. Place the reaction mixture(s) in a water bath at 30°C to promote the activity of any protease enzymes present. Take further absorbance
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