Author: Someya, Yuichi; Takeda, Naokazu; Miyamura, Tatsuo
Title: Characterization of the norovirus 3C-like protease Cord-id: ij5yaqkx Document date: 2005_3_8
ID: ij5yaqkx
Snippet: The recombinant 3C-like protease of Chiba virus, a Norovirus, expressed in Escherichia coli cells was purified and characterized as to effects of pH, temperature, salt contents, and SH reagents on its proteolytic activity. The optimal pH and temperature of the 3C-like protease for the proteolytic activity were 8.6 and 37 °C, respectively. Increased concentration (∼100 mM) of monovalent cations such as Na(+) and K(+) was inhibitory to the activity. Hg(2+) and Zn(2+) remarkably inhibited the pr
Document: The recombinant 3C-like protease of Chiba virus, a Norovirus, expressed in Escherichia coli cells was purified and characterized as to effects of pH, temperature, salt contents, and SH reagents on its proteolytic activity. The optimal pH and temperature of the 3C-like protease for the proteolytic activity were 8.6 and 37 °C, respectively. Increased concentration (∼100 mM) of monovalent cations such as Na(+) and K(+) was inhibitory to the activity. Hg(2+) and Zn(2+) remarkably inhibited the protease activity, while Mg(2+) and Ca(2+) had no virtual effect. Several sulfhydryl reagents such as p-chloromercuribenzoic acid, methyl methanethiosulfonate, N-ethylmaleimide and N-phenylmaleimide also blocked the activity, confirming the previous result that cysteine residue(s) were responsible for the proteolysis.
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