DNA polymerase I of the yeast Saccharomyces cerevisiae has been purified to near homogeneity. The enzyme sediments under high salt conditions as a band at 7.4 S and two polypeptides of Mr = 140,000 and 110,000 are resolved by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Both polypeptides react with rabbit anti-yeast DNA polymerase I serum and can be shown to be enzymatically active by renaturation in situ after electrophoresis on polyacrylamide gels in the presence of sodium dodecyl sulfate. This high molecular weight form of yeast DNA polymerase I is very sensitive to inhibition by aphidicolin. The biochemical properties of the enzyme and inhibitors that may aid in distinguishing yeast DNA polymerases I and II are also described.
Polypeptide structure of DNA polymerase I from Saccharomyces cerevisiae / G. Badaracco, L. Capucci, P. Plevani, L. M. Chang. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 258:17(1983 Sep 10), pp. 10720-6-10726.
|Titolo:||Polypeptide structure of DNA polymerase I from Saccharomyces cerevisiae|
PLEVANI, PAOLO (Penultimo)
|Parole Chiave:||Centrifugation, Density Gradient; Aphidicolin; Diterpenes; Electrophoresis, Polyacrylamide Gel; Protein Denaturation; DNA Polymerase II; Molecular Weight; Saccharomyces cerevisiae; DNA-Directed DNA Polymerase|
|Settore Scientifico Disciplinare:||Settore BIO/11 - Biologia Molecolare|
|Data di pubblicazione:||10-set-1983|
|Appare nelle tipologie:||01 - Articolo su periodico|