Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/80641
Type: Artigo de periódico
Title: INHIBITION OF THE WHEAT-GERM DNA POLYMERASE-A ACTIVITY BY THE ANTIVIRAL DRUG HPA-23
Author: AOYAMA, H
JUCA, MB
CASTROVIEJO, M
LITVAK, S
Abstract: Wheat germ DNA polymerase A, a gamma-like enzyme, recognized efficiently natural and synthetic RNA templates, resembling a retroviral reverse transcriptase (P. Laquel et al., Biochim Biophys Acta 1048 (1990):139-148). Ammonium-21-tungsto-9-antimoniate (HPA-23), an antiviral drug, inhibited the DNA polymerase A activities, independently of the template primers used, i.e. activated DNA or polyriboadenylic acid oligodeoxythymidylate (poly(rA)-oligo(dT)). The inhibition observed in the poly(rA)-oligo(dT)-directed DNA polymerase A activity occurred in the presence of either Mg2+, or Mn2+ as divalent cation, and also with the 2'-fluoro analogue of poly(rA) as template. HPA-23 was a noncompetitive inhibitor with respect to TTP, activated DNA, poly(rA)-oligo(dT), and poly(dAfl)-oligo(dT). A preincubation study showed a reversible HPA-23 binding to DNA polymerase A, in the presence of poly(rA)-oligo(dT) as the template primer.
Subject: DNA POLYMERASE-A
HPA-23
INHIBITION
WHEAT GERM
Country: Holanda
Editor: Kluwer Academic Publ
Rights: fechado
Identifier DOI: 10.1007/BF00021819
Date Issue: 1993
Appears in Collections:Unicamp - Artigos e Outros Documentos

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