DNA polymerase alpha and beta in the California urchin

Nucleic Acids Res. 1978 Oct;5(10):3945-57. doi: 10.1093/nar/5.10.3945.


DNA polymerase alpha and beta were identified in the urchin, Strongylocentrotus purpuratus. The DNA polymerase beta sedimented at 3.4 S, constituted 5% of total DNA polymerase activity, and was resistant to N-ethylmaleimide and high ionic strength. The polymerase alpha sedimented at 6--8 S, was inhibited by N-ethylmalemide or 0.1 M (NH4)2SO4, and was dependent upon glycerol for preservation of activity. Both the polymerases alpha and beta were nuclear associated in embryos. The DNA polymerase alpha was markedly heterogeneous on DEAE-Sephadex ion exchange and showed three modal polymerase species. These polymerase alpha species were indistinguishable by template activity assays but the DNA polymerase associated ribonucleotidyl transferase (Biochemistry 75 : 3106-3113, 1976) was found predominantly with only one of the DNA polymerase alpha species.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Nucleus / enzymology
  • DNA Replication / drug effects
  • DNA-Directed DNA Polymerase / isolation & purification*
  • DNA-Directed DNA Polymerase / metabolism
  • Female
  • Glycerol / pharmacology
  • Molecular Weight
  • Ovum / enzymology
  • Sea Urchins / embryology
  • Sea Urchins / metabolism*
  • Substrate Specificity
  • Templates, Genetic


  • DNA-Directed DNA Polymerase
  • Glycerol