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pubmed-article:12554059pubmed:abstractTextIt has been shown that the Hepatitis C virus nonstructural NS3 protein possesses at least two enzymatic domains: a serine-protease domain and an adenosine triphosphatase (ATPase)/helicase domain. In this report, a truncated fragment of NS3 (26 kDa), representing main epitopes from the (ATPase)/helicase domain, has been expressed in Escherichia coli. The recombinant protein was purified by Ion Metal Affinity Chromatography (IMAC) with more than 90% purity. The recognition of B-cell linear epitopes in the NS3 protein was evaluated by immunoblot. The recombinant NS3 protein was reduced and carboxymethylated, and the recognition of either conformational and/or linear B-cell determinants was evaluated by ELISA. The inclusion of the recombinant NS3 protein in a third-generation diagnostic system UltraMicroELISA (UMELISA) allowed an increase in the sensitivity, due to the detection of a new variety of false-negative sera in blood donor test samples.lld:pubmed
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pubmed-article:12554059pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:12554059pubmed:articleTitleAntigenicity of a recombinant NS3 protein representative of ATPase/helicase domain from hepatitis C virus.lld:pubmed
pubmed-article:12554059pubmed:affiliationDiagnostics Production Plant, Center for Genetic Engineering and Biotechnology, P.O. Box 6162, Havana 10600, Cuba.lld:pubmed
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