Purification and properties of a thermophilic and thermostable DNA polymerase from the archaebacterium Sulfolobus solfataricus.
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.
Rella
R
R
Istituto di Biochimica delle Proteine ed Enzimologia, CNR, Napoli.
Raia
C A
CA
Pisani
F M
FM
D'Auria
S
S
Nucci
R
R
Gambacorta
A
A
De Rosa
M
M
Rossi
M
M
D001105:Archaea / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D019384:Nucleic Acid Synthesis Inhibitors; D013379:Substrate Specificity; D013696:Temperature
D019384:Nucleic Acid Synthesis Inhibitors; D008345:Manganese; D004259:DNA-Directed DNA Polymerase; D008274:Magnesium