DNA polymerase α and β in the California urchin

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Abstract
DNA polymerase α and β were identified in the urchin, Strongylocentrotus purpuratus. The DNA polymerase β sedimented at 3.4 S, constituted 5% of total DNA polymerase activity, and was resistant to N-ethylmaleimide and high ionic strength. The polymerase α sedimented at 6-8 S, was inhibited by N-ethylmaleimide or 0.1 M (NH4)2SO4 and was dependent upon glycerol for preservation of activity. Both the polymerases α and β were nuclear associated in embryos. The DNA polymerase α was markedly heterogeneous on DEAE-Sephadex ion exchange and showed three modal polymerase species. These polymerase a 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 α species.