Highly Sensitive Protein Detection Based on Smart Hybrid Nanocomposite-Controlled Switch of DNA Polymerase Activity

2016 ◽  
Vol 8 (41) ◽  
pp. 28202-28207 ◽  
Author(s):  
Yue Huang ◽  
Hao Li ◽  
Lei Wang ◽  
Xiaoxia Mao ◽  
Genxi Li
Keyword(s):  
Dna Polymerase ◽  
Protein Detection ◽  
Polymerase Activity ◽  
Hybrid Nanocomposite ◽  
Highly Sensitive

scholarly journals Study of dogfish (Scyliorhinus caniculus) deoxyribonucleic acid polymerase α and β. Extraction, separation, characterization and changes during spermatogenesis

1980 ◽  
Vol 189 (3) ◽  
pp. 635-639 ◽  
Author(s):  
M Philippe ◽  
P Chevaillier
Keyword(s):  
Dna Polymerase ◽  
Sucrose Gradient ◽  
Deoxyribonucleic Acid ◽  
Dna Polymerases ◽  
Polymerase Activity ◽  
Polymerase Gamma ◽  
Polymerase Beta ◽  
Dna Polymerase Gamma ◽  
Highly Sensitive ◽  
Extraction Separation

DNA polymerase activity was extracted from testis cells of the dogfish Scyliorhinus caniculus. On a sucrose gradient, two main peaks could be separated, corresponding to DNA polymerases beta (3.8 S) and alpha (7.5 S). DNA polymerase gamma could also be detected when poly(A) . (dT)12 was used as template. The properties of alpha and beta polymerases of this primitive vertebrate were similar to those generally described, especially in mammals. The beta enzyme was highly sensitive to N-ethylmaleimide, however, and could use poly(dT) . poly(A) as template. Polymerase alpha was present in spermatogonia, spermatocytes and spermatids. Activity was maximal in spermatocytes. DNA polymerase beta was present in all testis cells with similar activities in spermatogonia and spermatocytes. Decreased activities were observed during spermiogenesis. Some activity remained associated with the chromatin fraction of mature sperm cells.

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 Mass Spectrometry versus Conventional Techniques of Protein Detection: Zika Virus NS3 Protease Activity towards Cellular Proteins

Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3732
Author(s):  
Agnieszka Dabrowska ◽  
Aleksandra Milewska ◽  
Joanna Ner-Kluza ◽  
Piotr Suder ◽  
Krzysztof Pyrc
Keyword(s):  
Mass Spectrometry ◽  
Zika Virus ◽  
Viral Infections ◽  
Protein Detection ◽  
Extensive Discussion ◽  
Protein Targets ◽  
Highly Sensitive ◽  
Infected Cells ◽  
Ns3 Protease ◽  
To Receive

Mass spectrometry (MS) used in proteomic approaches is able to detect hundreds of proteins in a single assay. Although undeniable high analytical power of MS, data acquired sometimes lead to confusing results, especially during a search of very selective, unique interactions in complex biological matrices. Here, we would like to show an example of such confusing data, providing an extensive discussion on the observed phenomenon. Our investigations focus on the interaction between the Zika virus NS3 protease, which is essential for virus replication. This enzyme is known for helping to remodel the microenvironment of the infected cells. Several reports show that this protease can process cellular substrates and thereby modify cellular pathways that are important for the virus. Herein, we explored some of the targets of NS3, clearly shown by proteomic techniques, as processed during infection. Unfortunately, we could not confirm the biological relevance of protein targets for viral infections detected by MS. Thus, although mass spectrometry is highly sensitive and useful in many instances, also being able to show directions where cell/virus interaction occurs, we believe that deep recognition of their biological role is essential to receive complete insight into the investigated process.

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
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