Purification and properties of a thermophilic and thermostable DNA polymerase from the archaebacterium Sulfolobus solfataricus

Ital J Biochem. 1990 Mar-Apr;39(2):83-99.


A DNA-dependent DNA polymerase was obtained in homogenous form from the thermoacidophilic archaebacterium Sulfolobus solfataricus. The enzyme, purified 706-fold, has a molecular mass of about 110000 daltons as determined by gel filtration and by glycerol gradient centrifugation. It requires Mg++ for its activity and has a pH optimum of 7.7. The activity is sharply dependent on the ionic strength. The enzyme is thermostable; its properties and activity requirements were characterized. The features of this enzyme are compared to those of other DNA polymerases isolated either from prokaryotes or eukaryotes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaea / enzymology*
  • Bacteria / enzymology*
  • DNA-Directed DNA Polymerase / isolation & purification*
  • DNA-Directed DNA Polymerase / metabolism
  • Hydrogen-Ion Concentration
  • Magnesium / pharmacology
  • Manganese / pharmacology
  • Molecular Weight
  • Nucleic Acid Synthesis Inhibitors
  • Substrate Specificity
  • Temperature


  • Nucleic Acid Synthesis Inhibitors
  • Manganese
  • DNA-Directed DNA Polymerase
  • Magnesium