Inhibition of Taq DNA polymerase by catalpol.

DNA polymerases have recently emerged as important cellular targets for chemical intervention in the development of anti-cancer agents. This report describes a PCR assay as a method to investigate the action mechanism of the inhibition of Taq DNA polymerase by catalpol. This inhibition was not prime...

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Detalhes bibliográficos
Autores: Pungitore, Carlos Rodolfo, Juri Ayub, Maximiliano, Borkowski, Eduardo Jorge, Tonn, Carlos Eugenio, Ciuffo, Gladys Maria
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2004
País:Argentina
Recursos:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/44638
Acesso em linha:http://hdl.handle.net/11336/44638
Access Level:acceso abierto
Palavra-chave:Dna Polymerases
Tumor Suppressor
Anticancer Agents
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
Descrição
Resumo:DNA polymerases have recently emerged as important cellular targets for chemical intervention in the development of anti-cancer agents. This report describes a PCR assay as a method to investigate the action mechanism of the inhibition of Taq DNA polymerase by catalpol. This inhibition was not primer or template specific, nor was it due to chelation of Mg2+ ions. In assays of hyperchromicity of double-stranded DNA, catalpol did not affect melting profile. The inhibitory effect of catalpol does not appear to depend on DNA concentration. In contrast, increasing dNTP concentration rescue the Taq DNA polymerase activity, suggestingthat catalpol acts in a competitive way with dNTPs at the binding site of the enzyme. Theoretical calculations reinforce the experimental data and the proposed mode of action of catalpol.