Abstract
Recombinant RNA-dependent RNA polymerase of hepatitis C virus was purified using a bacterial expression system (Escherichia coli). The system for enzyme activity detection was optimized. The maximum activity was achieved when the reaction was carried out at 30 degrees C in the presence of 3 mM Mg2+ or 0.75 mM Mn2+. Among alpha- and beta-pyrogallaldehydes, effective inhibitors were found. It was shown that they acted at the primer elongation stage, and their binding to the protein is reversible.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Hepacivirus / enzymology*
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Molecular Structure
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Protein Binding
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RNA-Dependent RNA Polymerase / antagonists & inhibitors*
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RNA-Dependent RNA Polymerase / genetics
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RNA-Dependent RNA Polymerase / metabolism
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Recombinant Proteins / antagonists & inhibitors
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Recombinant Proteins / metabolism
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Viral Proteins / antagonists & inhibitors*
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Viral Proteins / genetics
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Viral Proteins / metabolism
Substances
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Enzyme Inhibitors
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Recombinant Proteins
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Viral Proteins
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RNA-Dependent RNA Polymerase