Abstract
Fractionation of purified avian myeloblastosis virus DNA polymerase, after phosphorylation in vitro, revealed the presence of a small acidic protein, a phosphate acceptor polypeptide with high specific activity. Its presence in the phosphorylated form with the polymerase resulted in as much as a 10-fold increase in the rate of DNA synthesis. Its presence in the dephosphorylated form with the polymerase had no effect in the rate of DNA synthesis.
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Tsiapalis, C. Chemical modification of DNA polymerase phosphoprotein from avian myeloblastosis virus. Nature 266, 27–31 (1977). https://doi.org/10.1038/266027a0
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DOI: https://doi.org/10.1038/266027a0
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