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JBC, Vol. 251, Issue 4, 982-986, Feb, 1976
N. Battula and L. A. Loeb
Homogeneous DNA polymerase ("reverse transcriptase") from avian
myeoblastosis virus was assayed for exodeoxyribonuclease activity. The
substrates were defined template-initiator complexes in which different
radioactive nucleotides were present at the 3'-OH termini of the initiator.
Even when the number of molecules of enzyme was equal to the number of
initiator termini there was no significant release of radioactivity with
any of the template-initiator combinations tested. Under similar
conditions, the nuclease activity associated with either Escherichia coli
or T4DNA polymerases rendered more than 90% of the initiator termini
acid-soluble. The ratio of exodeoxyribonuclease activity to protein with
avian myeoblastosis DNA polymerase is less than 0.003% of that obtained
with E. coli DNA polymerase I. Furthermore, avian myeloblastosis virus DNA
polymerase failed to excise mispaired terminal nucleotides in both the
presence and absence of polymerization.
On the fidelity of DNA replication. Lack of exodeoxyribonuclease activity and error-correcting function in avian myeloblastosis virus DNA polymerase
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