| Literature DB >> 2113898 |
R Rella1, C A Raia, F M Pisani, S D'Auria, R Nucci, A Gambacorta, M De Rosa, M Rossi.
Abstract
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.Entities:
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Year: 1990 PMID: 2113898
Source DB: PubMed Journal: Ital J Biochem ISSN: 0021-2938