Inhibition of DNA polymerase alpha activity by ammonium 21-tungsto-9-antimoniate (HPA23)

Nucleic Acids Symp Ser. 1984;(15):169-72.

Abstract

Ammonium 21-tungsto-9-antimoniate (HPA23), an inorganic condensed ion, was shown to be a potent inhibitor for DNA polymerase alpha but not for beta. It inhibited the activity of mammalian DNA polymerase alpha in noncompetitive fashion with respect to either of deoxynucleotide substrate and template X primer, indicating the presence of a specific binding site for HPA23 on DNA polymerase alpha molecule. The Ki of the alpha polymerase for HPA23 was 24 nM. A possible interaction of HPA23 with DNA polymerase alpha is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antimony / pharmacology*
  • Antiviral Agents / pharmacology*
  • Burkitt Lymphoma
  • Cell Line
  • DNA Polymerase I / antagonists & inhibitors
  • DNA Polymerase II / antagonists & inhibitors*
  • Herpesvirus 4, Human / drug effects
  • Herpesvirus 4, Human / genetics
  • Humans
  • Kinetics
  • Mice
  • Plasmacytoma / enzymology
  • Tungsten / pharmacology*
  • Tungsten Compounds*

Substances

  • Antiviral Agents
  • Tungsten Compounds
  • ammonium tungsten antimonate hydroxide oxide
  • Antimony
  • DNA Polymerase I
  • DNA Polymerase II
  • Tungsten