[Isolation and characterization of DNA polymerase alpha, beta and gamma from the cells of the loach (Misgurnus fossilis)]

Biokhimiia. 1981 Sep;46(9):1539-47.
[Article in Russian]


Three DNA polymerases were partially purified from the embryos, liver and mitochondria of the loach Misgurnus fossilis by DEAE- and phosphocellulose chromatography and were identified as DNA polymerases alpha, beta and gamma. DNA polymerase alpha prefers the activated DNA as a template-primer and has a sedimentation value of 6.8S. The enzyme is stimulated by 50 mM potassium phosphate, KCl and, to a lesser extent, NaCl; has a pH optimum of 7.5 and is sensitive to N-ethylmaleimide. DNA polymerase beta also prefers the activated DNA as a template-primer but shows a sedimentation coefficient of 3.0 S. The enzyme is inhibited by salts and has a pH optimum of 8-9; its activity is rather resistant to N-ethylmaleimide. DNA polymerase gamma has a sedimentation value of 6.3S, shows a high activity on poly(A) . oligo(dT) in the presence of 100 mM potassium phosphate and a lesser activity in the presence of 150 mM KCl and NaCl. The enzyme has a pH optimum of 7.0.

MeSH terms

  • Animals
  • DNA Polymerase I / metabolism
  • DNA Polymerase II / metabolism
  • DNA Polymerase III / metabolism
  • DNA-Directed DNA Polymerase / isolation & purification
  • DNA-Directed DNA Polymerase / metabolism*
  • Embryo, Nonmammalian
  • Fishes
  • Kinetics
  • Liver / enzymology
  • Mitochondria / enzymology
  • Molecular Weight
  • Templates, Genetic


  • DNA Polymerase I
  • DNA Polymerase II
  • DNA Polymerase III
  • DNA-Directed DNA Polymerase