Facile and Sensitive Fluorescence Assay of DNA Polymerase Activity Using Cu2+ and Ascorbate as Signal Developers

2019 ◽  
Vol 4 (8) ◽  
pp. 2398-2403 ◽  
Author(s):  
Xingxing Zhang ◽  
Qiang Liu ◽  
Yan Jin ◽  
Baoxin Li
Keyword(s):  
Dna Polymerase ◽  
Polymerase Activity ◽  
Fluorescence Assay

Suggestive Evidence for an Oncorna-Virus-Specific DNA Polymerase from C-Type Particles of Bovine Leukosis

1974 ◽  
Vol 29 (1-2) ◽  
pp. 72-75 ◽  
Author(s):  
B. Dietzschold ◽  
O.R. Kaaden ◽  
S. Ueberschaer ◽  
F. Weiland ◽  
O. C. Straub
Keyword(s):  
Dna Polymerase ◽  
Polymerase Activity ◽  
Friend Virus ◽  
Leukaemia Virus ◽  
Virus Particles ◽  
Virus Rna ◽  
Feline Leukaemia Virus ◽  
Bovine Leukosis ◽  
Bovine Lymphocytes ◽  
Viral Preparation

Abstract Typical C-type oncorna virus particles as shown by electron microscopy have been purified from the supernatant of cultured lymphocytes from bovine leukosis. In the purified C-particle fraction a DNA-polymerase activity was detected. Using several synthetic RNA-or DNA-homopolymers and 70S Friend virus RNA the template response of this bovine leukosis cell particle DNA polymerase was compared with those of feline leukaemia virus DNA polymerase and DNA polymerase from normal bovine lymphocytes. The DNA polymerase detected in the viral preparation of bovine leukosis is suggested to be an oncorna-virus-specific enzyme.

scholarly journals Human Cytomegalovirus Inhibitor AL18 Also Possesses Activity against Influenza A and B Viruses

2012 ◽  
Vol 56 (11) ◽  
pp. 6009-6013 ◽  
Author(s):  
Giulia Muratore ◽  
Beatrice Mercorelli ◽  
Laura Goracci ◽  
Gabriele Cruciani ◽  
Paul Digard ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Dna Polymerase ◽  
Human Cytomegalovirus ◽  
Influenza A ◽  
Molecular Model ◽  
Polymerase Activity

ABSTRACTAL18, an inhibitor of human cytomegalovirus DNA polymerase, was serendipitously found to also block the interaction between the PB1 and PA polymerase subunits of influenza A virus. Furthermore, AL18 effectively inhibited influenza A virus polymerase activity and the overall replication of influenza A and B viruses. A molecular model to explain the binding of AL18 to both cytomegalovirus and influenza targets is proposed. Thus, AL18 represents an interesting lead for the development of new antivirals.

DNA polymerase activity of cultured normal and leukemic lymphocytes *1Response to phytohemagglutinin

1969 ◽  
Vol 57 (2-3) ◽  
pp. 257-262 ◽  
Author(s):  
Y RABINOWITZ ◽  
I MCCLUSKEY ◽  
P WONG ◽  
B WILHITE
Keyword(s):  
Dna Polymerase ◽  
Polymerase Activity

DNA Polymerase Activity in Human Serum: Studies with Australia Antigen

1973 ◽  
Vol 143 (2) ◽  
pp. 519-525 ◽  
Author(s):  
L. A. Loeb ◽  
R. O. Williams ◽  
A. I. Sutnick ◽  
A. O'Connell ◽  
I. Millman
Keyword(s):  
Human Serum ◽  
Dna Polymerase ◽  
Polymerase Activity ◽  
Australia Antigen

Detection and characterization of DNA polymerase activity in Toxoplasma gondii

Parasitology ◽  
1993 ◽  
Vol 107 (2) ◽  
pp. 135-139 ◽  
Author(s):  
A. Makioka ◽  
B. Stavros ◽  
J. T. Ellis ◽  
A. M. Johnson
Keyword(s):  
Toxoplasma Gondii ◽  
Dna Polymerase ◽  
Dna Polymerases ◽  
Sedimentation Coefficient ◽  
Polymerase Activity ◽  
Magnesium Ions ◽  
Dna Polymerase Β ◽  
Human Dna ◽  
Approximate Molecular Weight

SUMMARYA DNA polymerase activity has been detected and characterized in crude extracts from tachzoites of Toxoplasma gondii. The enzyme has a sedimentation coefficient of 6·4 S, corresponding to an approximate molecular weight of 150000 assuming a globular shape. Like mammalian DNA polymerase α, the DNA polymerase of T. gondii was sensitive to N-ethylmaleimide and inhibited by high ionic strength. However, the enzyme activity was not inhibited by aphidicolin which is an inhibitor of mammalian DNA polymerases α, δ and ε and also cytosine-β-D-arabinofuranoside-5′-triphosphate which is an inhibitor of α polymerase. The activity was inhibited by 2′,3′-dideoxythymidine-5′-triphosphate which is an inhibitor of mammalian DNA polymerase β and γ. Magnesium ions (Mg2+) were absolutely required for activity and its optimal concentration was 6 mM. The optimum potassium (K+) concentration was 50 mM and a higher concentration of K+ markedly inhibited the activity. Activity was optimal at pH 8. Monoclonal antibodies against human DNA polymerase did not bind to DNA polymerase of T. gondii. Thus the T. gondii enzyme differs from the human enzymes and may be a useful target for the design of toxoplasmacidal drugs.

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