147 resultados para glutathione peroxide


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This communication proposes the use of neural networks in the prediction of residual concentrations of hydrogen peroxide from the treatment of effluents through Advanced Oxidative Processes (AOP's), in particular, the photo-Fenton process. To verify the efficiency of the oxidative process, the Chemical Oxygen Demand (COD) parameter, the values of which may be modified by the presence of oxidizing agents such as residual hydrogen peroxide, is frequently taken in account. The analysis of the H2O2 interference was performed by spectrophotometry at 450 nm wavelength, via the monitoring of the reaction of ammonia with metavanadate. The results of the hydrogen peroxide residual concentration were modeled via a feedforward neural network, with the correlation coefficients between actual and predicted values above 0.96, indicating good prediction capacity.

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1. In order to investigate the effect of aging on the erythrocyte glutathione system, total glutathione (GSH), glutathione reductase (GSH-red) and glutathione peroxidase (GSH-px) levels were measured in erythrocytes from 33 young (mean age = 30.5 +/- 9.7 years) and 28 aged (mean age = 68.9 +/- 11.4 years) healthy individuals.2. GSH was 3.5 +/- 1.8-mu-M/g Hb for the young group, a value significantly greater (P < 0.01) than 2.3 +/- 0.9-mu-M/g Hb found for the aged group. Similarly, GSH-red activity, 5.5 +/- 1.8 IU/g Hb, was higher (P < 0.05) for the young group than 3.4 +/- 0.9 IU/g Hb found for the aged group. The GSH-px activity levels for the young group, 21.1 +/- 5.9 IU/g Hb, were significantly greater (P < 0.01) than 12.0 +/- 3.3 IU/g Hb for the aged group. The lower activity detected in the aged group for all of these parameters of the glutathione redox system was not related to low levels of hematocrit or hemoglobin.3. There was no statistical difference in the activation coefficient (AC) of reductase (+FAD/-FAD) between groups, which seems to indicate that the lower activity of glutathione reductase observed in the aged group was not due to riboflavin deficiency.4. Additional information is required to determine the mechanisms controlling the glutathione redox system and its role in the aging process.

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Several components of the erythrocyte-dependent glutathione redox system (reduced glutathione, GSH; oxidized glutathione, GSSG; glutathione peroxidase, GSH-Px; glutathione reductase, GSH-Red) were determined in patients with types I and II diabetes mellitus (DM). All groups studied were male subjects: G1, 20 young healthy individuals (aged 23.7 +/- 4.2 years); G2, 15 young insulin-treated type I DM patients; G3, 20 older insulin-treated type II DM patients; 04, 21 older oral hypoglycemic agent-treated type II DM patients; G5, 28 aged healthy individuals (aged 68.9 +/- 11.5 years). There were no differences between G1 and G2, G3 or G4 regarding erythrocyte GSH, GSSG, and GSH-Red (without FAD) levels. GSH-Px activity was significantly lower in G2 when compared to G1 (15.2 +/- 4.9 vs 20.6 +/- 6.6 IU/g Hb). The GSH-Red and GSH-Px activities and GSH levels were significantly higher in 03 (4.6 +/- 1.7 IU/g Hb, 20.2 +/- 8.7 IU/g Hb and 3.5 +/- 1.3-mu-M/g Hb) and G4 (5.0 +/- 2.2 IU/g Hb, 16.9 +/- 6.1 IU/g Hb and 5.0 +/- 2.3-mu-M/g Hb) when compared to G5 (3.4 +/- 0.9 IU/g Hb, 12.0 +/- 3.6 IU/g Hb and 2.3 +/- 0.9-mu-M/g Hb). The findings suggest that treatment of DM can stimulate the redox activity of red blood cells in aged subjects.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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In this communication we report a proof of concept study of the use of cyclic voltammetry with a polyeugenol-modified glassy carbon (GC) electrode to selectively detect L-cysteine in the presence of both DL-homocysteine and glutathione in perchloric acid. The formation of a polyeugenol-modified gold electrode is also reported for the first time.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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In this work, siloxane-poly(propylene oxide) discs (PPO disc) prepared using the sol-gel process were used as solid phase in enzyme-linked immunosorbent assays (ELISA) for the detection of anti-hepatitis C virus (HCV) antibodies. The HCV RNA from serum (genotype 1b) was submitted to the RT-PCR technique and subsequent amplification of the HCV core 408 pb. This fragment was cloned into expression vector pET42a and expressed in Escherichia coli as recombinant protein with glutathione S-transferase (GST). Cell cultures were grown and induced having a final concentration of 0.4 x 10(-3) mol L-1 of IPTG. After induction, the cells were harvested and the soluble fraction was analyzed using polyacrilamide gel 15% showing a band with an approximate molecular weight of 44 kDa, the expected size for this GST-fused recombinant protein. The recombinant protein was purified and continued by immunological detection using HCV-positive serum and showed no cross-reactivity with positive samples for other infectious diseases. An ELISA was established using 1.25 ng of recombinant protein per PPO disc, a dilution of 1: 10,000 and 1:40 for a peroxidase conjugate and serum, respectively, and solutions of hydrogen peroxide and 3,3',5,5'-tetra-methylbenzidine in a ratio of 1: 1. The proposed methodology was compared with the ELISA conventional polystyrene-plate procedure and the performance of the PPO discs as a matrix for immunodetection gave an easy synthesis, good performance and reproducibility for commercial application. (c) 2007 Elsevier B.V. All rights reserved.

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The aim of the present study was to evaluate the effect of 20% and 35% hydrogen peroxide bleaching gels on the color, opacity, and fluorescence of composite resins. Seven composite resin brands were tested and 30 specimens, 3-mm in diameter and 2-mm thick, of each material were fabricated, for a total of 210 specimens. The specimens of each tested material were divided into three subgroups (n=10) according to the bleaching therapy tested: 20% hydrogen peroxide gel, 35% hydroxide peroxide gel, and the control group. The baseline color, opacity, and fluorescence were assessed by spectrophotometry. Four 30-minute bleaching gel applications, two hours in total, were performed. The control group did not receive bleaching treatment and was stored in deionized water. Final assessments were performed, and data were analyzed by two-way analysis of variance and Tukey tests (p<0.05). Color changes were significant for different tested bleaching therapies (p<0.0001), with the greatest color change observed for 35% hydrogen peroxide gel. No difference in opacity was detected for all analyzed parameters. Fluorescence changes were influenced by composite resin brand (p<0.0001) and bleaching therapy (p=0.0016) used. No significant differences in fluorescence between different bleaching gel concentrations were detected by Tukey test. The greatest fluorescence alteration was detected on the brand Z350. It was concluded that 35% hydrogen peroxide bleaching gel generated the greatest color change among all evaluated materials. No statistical opacity changes were detected for all tested variables, and significant fluorescence changes were dependent on the material and bleaching therapy, regardless of the gel concentration.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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The aim of this study was to evaluate the amount of peroxide passage from the pulp chamber to the external enamel surface during the internal bleaching technique. Fifty bovine teeth were sectioned transversally 5 mm below the cemento-enamel junction (CEJ), and the remaining part of the root was sealed with a 2-mm layer of glass ionomer cement. The external surface of the samples was coated with nail varnish, with the exception of standardized circular areas (6-mm diameter) located on the enamel, exposed dentin, or cementum surface of the tooth. The teeth were divided into three experimental groups according to exposed areas close to the CEJ and into two control groups (n=10/group), as follows: GE, enamel exposure area; GC, cementum exposed area; GD, dentin exposed area; Negative control, no presence of internal bleaching agent and uncoated surface; and Positive control, pulp chamber filled with bleaching agent and external surface totally coated with nail varnish. The pulp chamber was filled with 35% hydrogen peroxide (Opalescence Endo, Ultradent). Each sample was placed inside of individual flasks with 1000 mu L of acetate buffer solution, 2 M (pH 4.5). After seven days, the buffer solution was transferred to a glass tube, in which 100 mu L of leuco-crystal violet and 50 mu L of horseradish peroxidase were added, producing a blue solution. The optical density of the blue solution was determined by spectrophotometer and converted into microgram equivalents of hydrogen peroxide. Data were submitted to Kruskal-Wallis and Dunn-Bonferroni tests (alpha=0.05). All experimental groups presented passage of peroxide to the external surface that was statistically different from that observed in the control groups. It was verified that the passage of peroxide was higher in GD than in GE (p<0.01). The GC group presented a significantly lower peroxide passage than did GD and GE (p<0.01). It can be concluded that the hydrogen peroxide placed into the pulp chamber passed through the dental hard tissues, reaching the external surface and the periodontal tissue. The cementum surface was less permeable than were the dentin and enamel surfaces.

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Xylella fastidiosa is an important pathogen bacterium transmitted by xylem-feedings leafhoppers that colonizes the xylem of plants and causes diseases on several important crops including citrus variegated chlorosis (CVC) in orange and lime trees. Glutathione-S-transferases (GST) form a group of multifunctional isoenzymes that catalyzes both glutathione (GSH)-dependent conjugation and reduction reactions involved in the cellular detoxification of xenobiotic and endobiotic compounds. GSTs are the major detoxification enzymes found in the intracellular space and mainly in the cytosol from prokaryotes to mammals, and may be involved in the regulation of stress-activated signals by suppressing apoptosis signal-regulating kinase 1. In this study, we describe the cloning of the glutathione-S-transferase from X. fastidiosa into pET-28a(+) vector, its expression in Escherichia coli, purification and initial structural characterization. The purification of recombinant xfGST (rxfGST) to near homogeneity was achieved using affinity chromatography and size-exclusion chromatography (SEC). SEC demonstrated that rxfGST is a homodimer in solution. The secondary and tertiary structures of recombinant protein were analyzed by circular dichroism and fluorescence spectroscopy, respectively. The enzyme was assayed for activity and the results taken together indicated that rxfGST is a stable molecule, correctly folded, and highly active. Several members of the GST family have been extensively studied. However, xfGST is part of a less-studied subfamily which yet has not been structurally and biochemically characterized. In addition, these studies should provide a useful basis for future studies and biotechnological approaches of rxfGST. (C) 2008 Elsevier B.V. All rights reserved.