Purification and properties of a thermophilic and thermostable DNA polymerase from the archaebacterium Sulfolobus solfataricus |
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| Authors: | R Rella C A Raia F M Pisani S D'Auria R Nucci A Gambacorta M De Rosa M Rossi |
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| Affiliation: | Istituto di Biochimica delle Proteine ed Enzimologia, CNR, Napoli. |
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| 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. |
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