Molecular size and fidelity of DNA polymerase alpha from the regenerating liver of the rat.
DNA-dependent DNA polymerase has been extracted from the soluble cytoplasmic fraction of regenerating rat liver and purified using phosphocellulose and DEAE-cellulose chromatography. Glycerol gradient analysis showed that the enzyme was predominantly DNA polymerase alpha, having a sedimentation coefficient of 10.5 S at low ionic strength and of 6--8 S at higher salt concentrations. The fidelity of purified enzyme was assessed using the co-polymer poly(dA-dT).poly(dA-dT) as a template for DNA synthesis. For both the aggregated (10.5 S) and disaggregated (6--8 S) forms, fidelities in the range of 1 wrong base in 100,000--150,000 complementary bases were obtained.
D000645:Ammonium Sulfate / Q000494:pharmacology; D000818:Animals; D004256:DNA Polymerase I / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008115:Liver Regeneration; D008297:Male; D008970:Molecular Weight; D009994:Osmolar Concentration; D051381:Rats; D012965:Sodium Chloride / Q000494:pharmacology; D013698:Templates, Genetic
D012965:Sodium Chloride; D004256:DNA Polymerase I; D004259:DNA-Directed DNA Polymerase; D000645:Ammonium Sulfate