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</script>doi: 10.1021/bi00607a037
pmid: 687572
dT1O will form triple-stranded complexes with dAn and these complexes can serve as substrate for T4 polynucleotide ligase (EC 6.5.1.1). The rate of phosphodiester formation was found to be approximately the same as for the double-stranded complex and, furthermore, the rate appears to be similar on the two strands in the complex. Joining of dT1O also took place in the presence of the double-stranded complexes dAn.dTn and dAn.rUn. Polyamines increase the rate of joining catalyzed by T4 polynucleotide ligase under certain conditions.
Kinetics, Polynucleotide Ligases, Polydeoxyribonucleotides, Oligodeoxyribonucleotides, Poly T, Poly dA-dT, Poly A, Coliphages, Substrate Specificity
Kinetics, Polynucleotide Ligases, Polydeoxyribonucleotides, Oligodeoxyribonucleotides, Poly T, Poly dA-dT, Poly A, Coliphages, Substrate Specificity
| citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 6 | |
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| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |
