Molecular size and fidelity of DNA polymerase alpha from the regenerating liver of the rat.
Salisbury, J G O'Connor, Peter J Saffhill, Roy
Salisbury, J G
O'Connor, Peter J
Saffhill, Roy
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Abstract
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.
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1978-01-26
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Molecular size and fidelity of DNA polymerase alpha from the regenerating liver of the rat. 1978, 517 (1):181-5 Biochim Biophys Acta