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  • Title: Purification and characterization of mouse DNA polymerase alpha devoid of primase activity.
    Author: Takada-Takayama R, Suzuki M, Enomoto T, Hanaoka F, Ui M.
    Journal: FEBS Lett; 1990 Oct 29; 273(1-2):27-30. PubMed ID: 2226860.
    Abstract:
    A simple method was developed for the isolation of primase-free DNA polymerase-alpha from the DNA polymerase-alpha-primase complex of mouse FM3A cells. The polymerase was separated from primase subunits by chromatography on a single-stranded DNA-cellulose column in the presence of 50% etylene glycol. The primase-free DNA polymerase-alpha contained two polypeptides with molecular masses of 180,000 and 68,000. Analysis of the DNA products with poly(dA)-oligo(dT)10 as template-primer revealed that both primase-free DNA polymerase-alpha and the DNA polymerase-alpha-primase complex predominantly synthesized short DNA with less than 30 nucleotides, but that the DNA polymerase-alpha-primase complex also synthesized some longer DNA with more than 300-400 nucleotides.
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