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Structural and Functional Properties of DNA Polymerase α from Calf Thymus

  • Friedrich Grummt
  • Waltraud Albert
  • Gerd Zastrow
  • Andrea Schnabel
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 179)

Abstract

DNA polymerase α, the enzyme most widely believed to catalyze chromosomal DNA replication in animal cells, is typically purified as a high molecular weight complex of multiple polypeptides, as revealed by SDS-polyacrylamide gel electrophoresis (1–11). The question of precise subunit structure of this enzyme and the structurefunction relationship of the individual polypeptides are subjects of our current research. We report here on the association of several functional properties -besides the catalytic DNA polymerizing activity- with the α-polymerase complex isolated from calf thymus, i.e. Ap4A binding, amino acyl tRNA synthetase, primase and 3′→5′ exonuclease- (proofreading-) activities.

Keywords

Exonuclease Activity High Molecular Weight Complex Nondenaturing Condition Hydroxyapatite Column Tryptic Peptide Mapping 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Friedrich Grummt
    • 1
  • Waltraud Albert
    • 1
  • Gerd Zastrow
    • 1
  • Andrea Schnabel
    • 1
  1. 1.Institut für BiochemieUniversität WürzburgWürzburgGermany

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