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PMID: 687572 Published · ppublish English Journal Article

T4 polynucleotide ligase catalyzed joining on triple-stranded nucleic acids.

Biochemistry ·Vol. 17 ·No. 14 ·1978-07-11 ·Pages 2939-42

Raae AJ, Kleppe K

Abstract

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.

MeSH Terms
Coliphages/enzymology Kinetics Oligodeoxyribonucleotides Poly A Poly T Poly dA-dT Polydeoxyribonucleotides Polynucleotide Ligases/metabolism Substrate Specificity
Chemicals
Oligodeoxyribonucleotides Polydeoxyribonucleotides Poly A Poly T Poly dA-dT Polynucleotide Ligases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Raae A J
Kleppe K
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1978-07-11
Pages
2939-42
Language
English
Region
United States
NLM ID
0370623
Subset
IM
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