scholarly journals The Enzymatic Activities of Nucleoside Triphosphate Diphosphohydrolases Towards Tenofovir Diphosphate and Their Spatial Distributions in Human Colorectal Tissue

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Herana Seneviratne ◽  
Craig Hendrix ◽  
Namandje Bumpus
Keyword(s):  
Enzymatic Activities ◽  
Nucleoside Triphosphate ◽  
Spatial Distributions ◽  
Colorectal Tissue ◽  
Tenofovir Diphosphate

scholarly journals Fluorescence Differentiation of ATP-Related Multiple Enzymatic Activities in Synovial Fluid as a Marker of Calcium Pyrophosphate Deposition Disease Using Kyoto Green

Molecules ◽  
2020 ◽  
Vol 25 (5) ◽  
pp. 1116
Author(s):  
Nattha Yongwattana ◽  
Nutsara Mekjinda ◽  
Tulyapruek Tawonsawatruk ◽  
Itaru Hamachi ◽  
Akio Ojida ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Synovial Fluid ◽  
Calcium Pyrophosphate ◽  
Enzymatic Activities ◽  
Nucleoside Triphosphate ◽  
Moderate Activity ◽  
Enzymatic Reactions ◽  
Calcium Pyrophosphate Deposition Disease ◽  
Deposition Disease ◽  
Nucleotide Pyrophosphatase

Calcium pyrophosphate deposition disease (CPPD) is a crystal induced inflammation in joints, and causes severe pain in elderly people. The accumulation of pyrophosphate (PPi) in synovial fluid (SF) results from several enzymatic reactions, especially the highly activated e-NPPs, which catalyze the conversion of ATP to PPi. This study demonstrates the detection of relative catalytic activity of 3 enzymes—ecto-nucleotide pyrophosphatase/phosphodiesterases (e-NPPs), tissue nonspecific alkaline phosphatase (TNAP), and ecto-nucleoside triphosphate diphosphohydrolases (e-NTPDases)—using a single molecular sensor called Kyoto Green. Kyoto Green exhibits excellent performance in sensing the catalytic activity of the commercial representatives of the e-NPPs, TNAP, and e-NTPDases, which are ENPP1, PPase, and apyrase, respectively, in both single-enzyme and multi-enzyme assays. Analysis of SF enzymes in 19 SF samples from human and swine revealed moderate activity of e-NPPs, high activity of e-NTPDases, and low activity of TNAP. Our newly developed method for analysis of multiple enzymatic activities using Kyoto Green in biological SF will assist improvement in accuracy of the CPPD prognosis/diagnosis, which will minimize unnecessary medical procedures.

scholarly journals The Helicase-Like Domain of Plant Potexvirus Replicase Participates in Formation of RNA 5′ Cap Structure by Exhibiting RNA 5′-Triphosphatase Activity

2001 ◽  
Vol 75 (24) ◽  
pp. 12114-12120 ◽  
Author(s):  
Yi-Ija Li ◽  
Ting-Wan Shih ◽  
Yau-Heiu Hsu ◽  
Yu-Tsung Han ◽  
Yih-Leh Huang ◽  
...  
Keyword(s):  
Enzymatic Activities ◽  
Nucleoside Triphosphate ◽  
Binding Motif ◽  
Helicase Domain ◽  
Cdna Fragment ◽  
Reading Frame ◽  
Metal Affinity ◽  
C Terminus ◽  
Capping Enzyme ◽  
Viral Replicase

ABSTRACT Open reading frame 1 (ORF1) of potexviruses encodes a viral replicase comprising three functional domains: a capping enzyme at the N terminus, a putative helicase in the middle, and a polymerase at the C terminus. To verify the enzymatic activities associated with the putative helicase domain, the corresponding cDNA fragment from bamboo mosaic virus (BaMV) was cloned into vector pET32 and the protein was expressed in Escherichia coli and purified by metal affinity chromatography. An activity assay confirmed that the putative helicase domain has nucleoside triphosphatase activity. We found that it also possesses an RNA 5′-triphosphatase activity that specifically removes the γ phosphate from the 5′ end of RNA. Both enzymatic activities were abolished by the mutation of the nucleoside triphosphate-binding motif (GKS), suggesting that they have a common catalytic site. A typical m7GpppG cap structure was formed at the 5′ end of the RNA substrate when the substrate was treated sequentially with the putative helicase domain and the N-terminal capping enzyme, indicating that the putative helicase domain is truly involved in the process of cap formation by exhibiting its RNA 5′-triphosphatase activity.

Reaction couples of ceramic thin films prepared by CVD

1988 ◽  
Vol 46 ◽  
pp. 798-799
Author(s):  
D.W. Susnitzky ◽  
S.R. Summerfelt ◽  
C.B. Carter
Keyword(s):  
Thin Film ◽  
Vapor Deposition ◽  
Chemical Vapor ◽  
Deposition Process ◽  
Solid State Reactions ◽  
Spatial Distributions ◽  
Diffusion Couples ◽  
Kinetics Studies ◽  
Ceramic Thin Films ◽  
Initial Stage

Solid-state reactions have traditionally been studied in the form of diffusion couples. This ‘bulk’ approach has been modified, for the specific case of the reaction between NiO and Al2O3, by growing NiAl2O4 (spinel) from electron-transparent Al2O3 TEM foils which had been exposed to NiO vapor at 1415°C. This latter ‘thin-film’ approach has been used to characterize the initial stage of spinel formation and to produce clean phase boundaries since further TEM preparation is not required after the reaction is completed. The present study demonstrates that chemical-vapor deposition (CVD) can be used to deposit NiO particles, with controlled size and spatial distributions, onto Al2O3 TEM specimens. Chemical reactions do not occur during the deposition process, since CVD is a relatively low-temperature technique, and thus the NiO-Al2O3 interface can be characterized. Moreover, a series of annealing treatments can be performed on the same sample which allows both Ni0-NiAl2O4 and NiAl2O4-Al2O3 interfaces to be characterized and which therefore makes this technique amenable to kinetics studies of thin-film reactions.

Application of high-resolution field-emission LVSEM, backscatter imaging, immunogold staining to definition of the spatial distributions of two human neutrophil adherence receptors

1993 ◽  
Vol 51 ◽  
pp. 36-37
Author(s):  
Robert D. Nelson ◽  
Sharon R. Hasslen ◽  
Stanley L. Erlandsen
Keyword(s):  
Cell Surface ◽  
Surface Membrane ◽  
Three Dimensional ◽  
Human Neutrophils ◽  
Spatial Distributions ◽  
Immunogold Staining ◽  
Functional Control ◽  
Neutrophil Adherence ◽  
Definition Of ◽  
Mode Of Attachment

Receptors are commonly defined in terms of number per cell, affinity for ligand, chemical structure, mode of attachment to the cell surface, and mechanism of signal transduction. We propose to show that knowledge of spatial distribution of receptors on the cell surface can provide additional clues to their function and components of functional control.L-selectin and Mac-1 denote two receptor populations on the neutrophil surface that mediate neutrophil-endothelial cell adherence interactions and provide for targeting of neutrophil recruitment to sites of inflammation. We have studied the spatial distributions of these receptors using LVSEM and backscatter imaging of isolated human neutrophils stained with mouse anti-receptor (primary) antibody and goat anti-mouse (secondary) antibody conjugated to 12 nm colloidal gold. This combination of techniques provides for three-dimensional analysis of the expression of these receptors on different surface membrane domains of the neutrophil: the ruffles and microvilli that project from the cell surface, and the cell body between these projecting structures.

Differentiation of Tumour from Normal Colorectal Tissue by SELDI-MS Protein Profiling

Endoscopy ◽  
2004 ◽  
Vol 36 (05) ◽  
Author(s):  
AM Lennon ◽  
D Stuart ◽  
AC Tan ◽  
E Fox ◽  
KS Sheahan ◽  
...  
Keyword(s):  
Protein Profiling ◽  
Colorectal Tissue ◽  
Normal Colorectal Tissue
Sign in / Sign up

Export Citation Format

Share Document