Abstract
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.
MeSH Terms
Animals
Cell Nucleus/enzymology
DNA Replication/drug effects
DNA-Directed DNA Polymerase/isolation & purification,metabolism
Female
Glycerol/pharmacology
Molecular Weight
Ovum/enzymology
Sea Urchins/embryology,metabolism
Substrate Specificity
Templates, Genetic
Chemicals
DNA-Directed DNA Polymerase
Glycerol
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Racine F M
Morris P W
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26 references, click to expand
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