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. 1985 Feb 25;13(4):1239–1249. doi: 10.1093/nar/13.4.1239

Characterization of a 3'----5' exonuclease activity in the phage phi 29-encoded DNA polymerase.

L Blanco, M Salas
PMCID: PMC341069  PMID: 2987819

Abstract

Purified protein p2 of phage phi 29, characterized as a specific DNA polymerase involved in the initiation and elongation of phi 29 DNA replication, contains a 3'----5' exonuclease active on single-stranded DNA, but not on double-stranded DNA. No 5'----3' exonuclease activity was found. The 3'----5' exonuclease activity was shown to be associated with the DNA polymerase since 1) the two activities were heat-inactivated with identical kinetics and 2) both activities, present in purified protein p2, cosedimented in a glycerol gradient.

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Selected References

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