DNA polymerase alpha and beta in the California urchin.
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.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D004261:DNA Replication / Q000187:drug effects; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification* / Q000378:metabolism; D005260:Female; D005990:Glycerol / Q000494:pharmacology; D008970:Molecular Weight; D010063:Ovum / Q000201:enzymology; D012617:Sea Urchins / Q000196:embryology / Q000378:metabolism*; D013379:Substrate Specificity; D013698:Templates, Genetic
D004259:DNA-Directed DNA Polymerase; D005990:Glycerol