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- W1975028636 abstract "Abstract Bacteriophage T5-induced DNA polymerase has an associated 3′→5′ exonuclease activity for which both single-stranded and duplex DNA serve as substrate (1). In this report, we demonstrate that hydrolysis of single-stranded DNA homopolymers (template) is inhibited in the presence of complementary (Watson-Crick sense) oligonucleotides (primer). Almost complete inhibition is observed at a primer/template ratio of ⋍ 0.1. Formation of “H-bonded” primer-template complex seems to be necessary for the inhibition of template hydrolysis because (a) similar amounts of noncomplementary oligonucleotides have no detectable effect on the rate of template hydrolysis, and (b) complementary oligonucleotides lose their inhibitory potential at temperatures where the H-bonded primer-template complex is expected to be unstable. From our data, it appears that the inhibition of template hydrolysis in the presence of primer molecules is due to the preferential binding of the enzyme at the 3′-OH terminus of the primer in the primer-template complex." @default.
- W1975028636 created "2016-06-24" @default.
- W1975028636 creator A5040321485 @default.
- W1975028636 date "1977-11-01" @default.
- W1975028636 modified "2023-09-26" @default.
- W1975028636 title "Primer-mediated inhibition of the hydrolysis of template DNA by T5-induced DNA polymerase" @default.
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- W1975028636 doi "https://doi.org/10.1016/0006-291x(77)90087-0" @default.
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