Results 151 to 160 of about 3,900 (192)
Purification and properties of a soluble polynucleotide ligase from chick embryo
Biochimie, 1977 J.C. David
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Effect of ATP analogues on T4 polynucleotide ligase
Biochemical and Biophysical Research Communications, 1978Abstract The influence of three ATP analogues, α, β-methylene adenosine 5′-triphosphate, β, γ-methylene adenosine 5′-triphosphate and β, γ-imidoadenosine 5′-triphosphate on the activity of T 4 polynucleotide ligase has been investigated. Only β, γ-imidoadenosine 5′-triphosphate was active in the joining reaction; the rate of catalysis being slightly
A J, Raae, K, Kleppe
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Polynucleotide cellulose as a substrate for a polynucleotide ligase induced by phage T4
Biochemical and Biophysical Research Communications, 1967Abstract An enzyme which joins polydeoxynucleotide strands has been identified in and purified from extracts Escherichia coli infected with phage T4 am N82 and appears to be the same as the ligase described by Weiss and Richardson. A novel method for detecting and assaying such enzymes involves the joining of a strand to one that is ...
N R, Cozzarelli +3 more
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A new method of assay for polynucleotide ligase
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1974Abstract A new method for the assay of polynucleotide ligase is described. It consists of two parallel DNA polymerase reactions with poly(dA) · oligo(dT) as template-primer and d[3H] TTP as precursor; ligase is added to both, but one is supplemented with NMN and the other with NAD.
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Intergenic suppression of amber polynucleotide ligase mutation in bacteriophage T4
Virology, 1970Abstract An intergenic suppressor ( m ) of the amber ligase mutation ( amH 39 x ) was isolated and a number of possible mechanisms of suppression were investigated. The intergenic suppressor does not appear to involve suppression of the amber codon.
V L, Chan, S, Shugar, K, Ebisuzaki
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Induction of polynucleotide ligase in human lymphocytes stimulated by phytohemoagglutinin
Biochemical and Biophysical Research Communications, 1972Abstract The treatment of human lymphocytes with phytohemoagglutinin causes the appearance of the activity of polynucleotide ligase, rising at least 50 fold from levels below the background. This increase takes place in the fourth or fifth day after treatment, and is delayed by one day approximately with respect to the rise of DNA synthesis rate; the
A M, Pedrini +4 more
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The activity of mammalian polynucleotide ligase on X-irradiated DNAs
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1978Selected samples of heterogeneous DNA from calf thymus with similar number-average molecular weight, Mn, and a low incidence of single-strand breaks were exposed in aqueous solutions to a mild X-ray dose of 1500 rads. The irradiation produced on the average about 0.2 bihelical and 2.2 monohelical scissions per DNA molecule of 1708 000 Mn.
M, Mathelet +3 more
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A biological assay for polynucleotide ligase: Recovery of marker activity in DNA-transformation
Biochemical and Biophysical Research Communications, 1967 Ekkehard K.F. Bautz
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Purification and properties of a polynucleotide ligase from calf thymus glands
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1972Abstract Polynucleotide ligase has been purified over 390-fold from extracts of calf thymus glands. A solid-state model of DNA containing single-strand breaks, namely, the poly(dA) · [poly([ 3 H]dT)-poly(dT)]-cellulose, was used as substrate for the enzymatic assays.
BERTAZZONI, Umberto +2 more
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The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases
Current Opinion in Structural Biology, 2004ATP- and NAD(+)-dependent DNA ligases, ATP-dependent RNA ligases and GTP-dependent mRNA capping enzymes comprise a superfamily of proteins that catalyze nucleotidyl transfer to polynucleotide 5' ends via covalent enzyme-(lysyl-N)-NMP intermediates. The superfamily is defined by five peptide motifs that line the nucleotide-binding pocket and contribute ...
Stewart, Shuman, Christopher D, Lima
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