Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1832588 (PSS)
 2,979 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Anti-endothelial cell antibodies (AECA) have been detected in autoimmune diseases such as systemic lupus erythematosus (SLE) and scleroderma (PSS) but their role in pathogenesis is unknown. Immunofluorescence, immunohistochemistry, complement-dependent antibody lysis, and radioimmunoassay have been used in the past to detect AECA. We have developed a rapid, sensitive, and quantitative cellular enzyme-linked immunosorbent assay (ELISA) to detect and characterize AECA. Sera were obtained from 28 normal volunteers, 28 patients with SLE, and 14 patients with PSS. We also performed studies in 47 patients with various monoclonal gammopathies. Endothelial cells (EC) were obtained from human umbilical veins by standard methods and subcultured on 96-well tissue culture plates without fixation. EC were then sequentially incubated with sera, peroxidase-conjugated goat anti-human Ig (IgG, IgM, or IgA), and substrate. Optical density readings were converted to arbitrary units by developing a standard curve. Heavy-chain specific antibodies were used to determine the class of AECA binding to EC. IgG was purified by using protein A columns and digested with pepsin to obtain F(ab')2 fragments. The mean units of AECA from normals were 19.3 for IgG and 12.5 for IgM. SLE sera showed significant levels of IgM AECA (37 units, P less than 0.001) but not IgG (29 units, P less than 0.1). PSS sera showed significant levels of both IgM AECA (38 units, P = 0.001) and IgG AECA (42.7 units, P less than 0.005). IgA AECA were not detected in normal, SLE, or PSS sera. Blocking Fc receptors with rabbit IgG did not affect the titer of IgG or IgM AECA.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Anti-endothelial cell antibodies: detection and characterization using a cellular enzyme-linked immunosorbent assay. 354 64

We have utilized the highly conducting poly(3,4-ethylenedioxythiophene)/poly(styrenesulfonate) aqueous dispersion (PEDOT/PSS) to build a conducting hydrogel matrix. Together with appropriate biomolecules this constitutes a hydrogel bio-electrode. The open hydrogel structure makes diffusion of analytes surrounding the cells into the matrix electrode easier. If enzymes are utilized, osmium is used as mediator between the prosthetic group of the enzyme and the conducting polymer matrix. Osmium also functions as a crosslink point to poly-4-vinylpyridine, which together with the magnesium crosslinked PEDOT/PSS gives a rigid hydrogel. The enzyme Horseradish peroxidase (HRP) was used as a model enzyme to evaluate the enzyme-enhanced electrode. We evaluated the electrode at pH 7, which is the pH choice for many biological systems. From cyclic voltammetry (CV) measurements we deduced that a very low reduction potential was needed to reduce the prosthetic group. Constant potential amperometry were performed to demonstrate the biosensor capabilities. A differential sensitivity of 0.13 A M(-1) cm(-2) through the 0-30 microM concentration range was achieved. Both the biostability and the influence on conductivity, important aspects when for example making nerve- or cell-electrodes, were investigated.
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PMID:Hydrogels of a conducting conjugated polymer as 3-D enzyme electrode. 1461 55

Stable electroactive films were grown layer by layer on rough pyrolytic graphite electrodes featuring 4-nm underlayers of sulfonated polyaniline (SPAN) covered with a film containing myoglobin or horseradish peroxidase grown in alternating layers with poly(styrenesulfonate). The self-doped polyanionic SPAN layer, grown on a 2-nm polycation layer, was conductive between about 0.1 and -0.4 V vs SCE at pH 4.5. The enzyme films had the architecture PDDA/SPAN/(enzyme/PSS)3, where PDDA is poly(diallyldimethylammonium) ion. Comparisons of voltammetric measurements of electroactive protein with quartz crystal microbalance measurements of total protein showed that 90% or more of the protein was coupled to the electrode when the SPAN underlayer was present, as opposed to approximately 40% protein electroactivity when SPAN was absent. As a consequence of the highly efficient coupling between enzymes and electrode, the PDDA/SPAN/(enzyme/PSS)3 films exhibited a higher sensitivity for the electrochemical catalytic reduction of hydrogen peroxide. Amperometry at a rotating disk electrode at 0 V gave sensitivity for hydrogen peroxide up to 14 microA microM(-1) cm(-2) in the submicromolar concentration range and a detection limit of approximately 3 nM. Results suggest the future utility of ultrathin layers of conductive self-doping polyions in improving sensitivity of enzyme biosensors.
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PMID:Wiring of enzymes to electrodes by ultrathin conductive polyion underlayers: enhanced catalytic response to hydrogen peroxide. 1463 65

The influence of a catalase (Cat) layer located at different depths in the layer-by-layer hemoglobin/polystyrene sulfonate films with an (Hb/PSS)(20)(-)(x)/(Cat/PSS)/(Hb/PSS)(x) (x = 0-20) architecture on kinetics of hemoglobin degradation under treatment with hydrogen peroxide solutions of different concentrations and features of H(2)O(2) decay in surrounding solutions has been studied. While assembled on the top of the multilayers, the catalase layer shows the highest activity in hydrogen peroxide decomposition. Hemoglobin in such films retains its nativity for a longer period of time. The effect of catalase layers is compared with that of protamine, horseradish peroxidase, and inactivated catalase. Positioning an active layer with catalytic properties as an outer layer is the best protection strategy for layer-by-layer assembled films in aggressive media.
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PMID:Layer-by-layer enzyme/polyelectrolyte films as a functional protective barrier in oxidizing media. 1686 52

Molecular films of protein/polyion layers were assembled by means of alternate adsorption through electrostatic interaction. Glucose oxidase (GOD) and peroxidase (POD) were assembled in combination with sodium poly(styrenesulfonate) (PSS) and poly(ethyleneimine) (PEI), respectively. Enzyme activities of those films on specific substrates (glucose and H(2)O(2)) were examined by coloring reaction of dye DA67. A multienzyme film containing GOD layer and POD layer was prepared by alternate adsorption of POD/PSS followed by PEI/GOD. Sequential redox reaction of glucose/H(2)O(2)/DA67 was demonstrated successfully with this supramolecular system.
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PMID:Sequential actions of glucose oxidase and peroxidase in molecular films assembled by layer-by-layer alternate adsorption. 1862 25

This paper describes the use of horseradish peroxidase (HRP) based biosensor for novel detection of glyphosate herbicide. The biosensor was prepared by electrochemically depositing poly(2,5-dimethoxyaniline) (PDMA) doped with poly(4-styrenesulfonic acid) (PSS) onto the surface of a gold electrode followed by electrostatic attachment of the enzyme HRP onto the PDMA-PSS composite film. Fourier transform infrared (FTIR) and UV-Vis spectrometry inferred that HRP was not denatured during its immobilization on PDMA-PSS composite film. The biosensing principle was based on the determination of the cathodic responses of the immobilized HRP to H(2)O(2), before and after incubation in glyphosate standard solutions. Glyphosate inhibited the activity of HRP causing a decrease in its response to H(2)O(2). The determination of glyphosate was achieved in the range of 0.25-14.0 microg L(-1) with a detection limit of 1.70 microg L(-1). The apparent Michaelis-Menten constant (calculated for the HRP/PDMA-PSS biosensor in the presence and absence of glyphosate was found to be 7.73 microM and 7.95 microM respectively.
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PMID:Electrochemical detection of glyphosate herbicide using horseradish peroxidase immobilized on sulfonated polymer matrix. 1933 72

Using zinc powders as source material, ZnO nanorods (ZnONR) were fabricated on gold wire by a hydrothermal reaction without any other surfactant. The gold wire end was coated by a thin layer of Zn-Au alloy to improve the nucleation for growth of ZnO nanostructures and to further improve the performance of the biosensor, which was constructed by alternatively immobilizing poly(sodium 4-styrenesulfonate) (PSS) and horseradish peroxidase (HRP) on the ZnONR. Electrochemical measurement, ultraviolet-visible spectrum, zeta-potential, and scanning electron microscopic analysis demonstrated that PSS and HRP were stably adsorbed layer by layer on the ZnONR surface, and the HRP kept bioactivity for H(2)O(2) detection without an electron transfer mediator. The multilayered HRP sensors exhibited a wide linear range and low detection limit. The sensitivity of the biosensor increased with the immobilized HRP layers from the lowest value of 36.28 microA mM(-1) for a monolayer.
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PMID:Layer by layer immobilized horseradish peroxidase on zinc oxide nanorods for biosensing. 1935 42

Self-assembly methods for the immobilisation or encapsulation of the positively charged redox protein, cytochrome c (cyt c), in layered organoclays or silica nanoparticles, respectively, are described and contrasted. Protein-polymer-organoclay nanocomposites are produced by spontaneous restacking of delaminated aminopropyl-functionalised magnesium phyllosilicate sheets in the presence of an aqueous solution of poly(sodium 4-styrene sulfonate) (PSS) and cyt c. In contrast, single molecules of cyt c are encapsulated in silica nanoparticles by sol-gel reactions at the oil-water interface of microemulsion water droplets. In both cases, the protein molecules remain structurally intact after entrapment, are accessible to small molecule redox agents, exhibit excellent peroxidase activity in the presence of hydrogen peroxide, and show enhanced stability and catalytic properties under adverse conditions of pH. The ability to prepare functional protein-inorganic conjugates in general could significantly extend the technological scope of biological products and processes, and should therefore be an important adjunct in the translation of synthetic biology to real-life applications.
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PMID:Immobilisation and encapsulation of functional protein-inorganic constructs. 1956 13

A highly soluble poly(3,4-ethylenedioxythiophene)-poly(styrene sulfonic acid)/Au (PEDOT-PSS/Au) nanocomposite was prepared via one-step chemical synthesis and the matrix was characterized by UV-vis spectroscopy (UV-vis), Fourier transform infrared spectroscopy (FT-IR), scanning electron microscope (SEM) and transmission electron microscope (TEM). Due to the excellent aqueous compatibility and biocompatibility, the PEDOT/PSS-Au nanocomposite can be used as biomaterial for enzymes immobilization. In this system, redox enzyme, horseradish peroxidase (HRP) was integrated with PEDOT/PSS-Au nanocomposite and the direct electron transfer of HRP was observed. Moreover, we find that the HRP/PEDOT-PSS/Au modified electrode shows excellent electrocatalytic ability for H(2)O(2) and the formal Michaelis-Menten constant (K(m)(app)) was 0.78 mmol/L. The response currents have good linear relation with the concentrations of H(2)O(2) with a linear range from 2.0 x 10(-7) to 3.8 x 10(-4)mol/L.
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PMID:A highly soluble poly(3,4-ethylenedioxythiophene)-poly(styrene sulfonic acid)/Au nanocomposite for horseradish peroxidase immobilization and biosensing. 2080 65

Piezoelectric inkjet printing of polymers and proteins holds great promise for fabrication of miniaturized bioelectronic devices, such as biochips and biosensors. In this study, a bienzymatic glucose biosensor prototype based on poly(3,4-ethylenedioxythiophene)-poly(styrene sulfonic acid) (PEDOT-PSS), glucose oxidase (GOD), and horseradish peroxidase (HRP) was fabricated by a piezoelectric inkjet printer. An aqueous bioelectrical ink containing PEDOT-PSS, GOD, and HRP was prepared and printed on an indium-tin-oxide (ITO)-coated poly(ethylene terephthalate) (PET) film. The PEDOT-PSS/GOD/HRP sensor was covered with a cellulose acetate membrane. The use of bienzymatic sensing combined with conducting polymers via piezoelectric inkjet printing showed a synergistic effect resulting in significant amplification of the response signal. The glucose sensor reached steady-state current density within 3 s, indicating a fast response time, and exhibited a linear dose-dependent electrochemical response with high sensitivity. The overall result demonstrates that a glucose sensor with high sensitivity could be readily fabricated by a piezoelectric inkjet printing system.
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PMID:A glucose sensor fabricated by piezoelectric inkjet printing of conducting polymers and bienzymes. 2147 12


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