Search results for "peroxidases"

showing 10 items of 26 documents

Interference of carbidopa and other catechols with reactions catalyzed by peroxidases

2018

Abstract Background A number of compounds, including ascorbic acid, catecholamines, flavonoids, p-diphenols and hydrazine derivatives have been reported to interfere with peroxidase-based medical diagnostic tests (Trinder reaction) but the mechanisms of these effects have not been fully elucidated. Methods Reactions of bovine myeloperoxidase with o-dianisidine, bovine lactoperoxidase with ABTS and horseradish peroxidase with 4-aminoantipyrine/phenol in the presence of carbidopa, an anti-Parkinsonian drug, and other catechols, including l -dopa, were monitored spectrophotometrically and by measuring hydrogen peroxide consumption. Results Chromophore formation in all three enzyme/substrate sy…

0301 basic medicineParkinson's diseaseBiophysicsCatecholsperoxidaseBiochemistryHorseradish peroxidaseCatalysis03 medical and health scienceschemistry.chemical_compoundmedicineAnimalsHumansLactoperoxidasecarbidopaHydrogen peroxideenzymatic assay interferenceMolecular BiologyHorseradish PeroxidaseCatecholABTS030102 biochemistry & molecular biologybiologyMolecular StructureMonophenol MonooxygenaseLactoperoxidasehydrazineHydrogen PeroxidecatecholAscorbic acidCombinatorial chemistryMolecular Docking Simulation030104 developmental biologychemistryChromogenic CompoundsPeroxidasesCarbidopabiology.proteinParkinson’s diseaseCattleOxidation-Reductionmedicine.drugPeroxidaseBiochimica et Biophysica Acta-General Subjects
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Correlation between superoxide dismutase, glutathione peroxidase and catalase in isolated rat hepatocytes during fetal development

1981

Abstract Superoxide dismutase, glutathione peroxidase and catalase activities were determined in isolated fetal rat hepatocytes of various ages and compared with the values of neonatal and adult cells. The developmental pattern of superoxide dismutase and glutathione peroxidase were very similar with a low constant activity in the fetal cells and a postnatal burst. On the contrary catalase begins to increase already since the 18th day of the fetal life. The results suggest a functional correlation of superoxide dismutase and glutathione peroxidase in the antioxidative enzyme defense of liver cells.

AgingGPX3BiophysicsGestational AgeAntioxidative enzymeSettore BIO/09BiochemistryGPX5GPX6Superoxide dismutaseFetusPregnancyAnimalsMolecular Biologychemistry.chemical_classificationGlutathione PeroxidaseFetusbiologySuperoxide DismutaseChemistryGlutathione peroxidaseRats Inbred StrainsCell BiologyCatalaseRatsAnimals NewbornLiverPeroxidasesBiochemistryCatalasebiology.proteinFemaleBiochemical and Biophysical Research Communications
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Melatonin activates the peroxidase-oxidase reaction and promotes oscillations.

2001

We have studied the peroxidase-oxidase reaction with NADH and O2 as substrates and melatonin as a cofactor in a semibatch reactor. We show for the first time that melatonin is an activator of the reaction catalyzed by enzymes from both plant and animal sources. Furthermore, melatonin promotes oscillatory dynamics in the pH range from 5 to 6. The frequency of the oscillations depends on the pH such that an increase in pH was accompanied by a decrease in frequency. Conversely, an increase in the flow rate of NADH or an increase in the average concentration of NADH resulted in an increase in oscillation frequency. Complex dynamics were not observed with melatonin as a cofactor. These results a…

BiophysicsBiochemistryHorseradish peroxidaseCofactorCatalysisMelatoninOscillometrymedicineAnimalsLactoperoxidaseMolecular BiologyHorseradish PeroxidaseMelatoninchemistry.chemical_classificationOxidase testbiologyChemistryLactoperoxidaseCell BiologyHydrogen-Ion ConcentrationNADOxygenKineticsEnzymeMilkBiochemistryModels ChemicalPeroxidasesbiology.proteinCattleNAD+ kinaseSoybeansOxidoreductaseshormones hormone substitutes and hormone antagonistsPeroxidasemedicine.drugBiochemical and biophysical research communications
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Vanadium pentoxide nanoparticles mimic vanadium haloperoxidases and thwart biofilm formation

2012

Marine biofouling—the colonization of small marine microorganisms on surfaces that are directly exposed to seawater, such as ships' hulls—is an expensive problem that is currently without an environmentally compatible solution1. Biofouling leads to increased hydrodynamic drag, which, in turn, causes increased fuel consumption and greenhouse gas emissions. Tributyltin-free antifouling coatings and paints1, 2, 3, 4 based on metal complexes or biocides have been shown to efficiently prevent marine biofouling. However, these materials can damage5 the environment through metal leaching (for example, of copper and zinc)6 and bacteria resistance7. Here, we show that vanadium pentoxide nanowires ac…

BromidesBiocideVanadium CompoundsBiofoulingBiomedical Engineeringchemistry.chemical_elementVanadiumBioengineeringZincBiofoulingchemistry.chemical_compoundHypobromous acidHumansPentoxideSeawaterGeneral Materials ScienceElectrical and Electronic EngineeringHydrogen peroxideShipsSinglet OxygenNanowiresChemistryHydrogen PeroxideCondensed Matter PhysicsCopperAtomic and Molecular Physics and OpticsAnti-Bacterial AgentsPeroxidasesChemical engineeringBiofilmsNanoparticlesNature Nanotechnology
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Insights into how nucleotide supplements enhance the peroxidase-mimicking DNAzyme activity of the G-quadruplex/hemin system

2012

Since the initial discovery of the catalytic capability of short DNA fragments, this peculiar enzyme-like property (termed DNAzyme) has continued to garner much interest in the scientific community because of the virtually unlimited applications in developing new molecular devices. Alongside the exponential rise in the number of DNAzyme applications in the last past years, the search for convenient ways to improve its overall efficiency has only started to emerge. Credence has been lent to this strategy by the recent demonstration that the quadruplex-based DNAzyme proficiency can be enhanced by ATP supplements. Herein, we have made a further leap along this path, trying first of all to deci…

DeoxyribozymeNanotechnologyBiology010402 general chemistryG-quadruplex01 natural sciencesCatalysischemistry.chemical_compoundAdenosine TriphosphateGeneticsNucleotideCatalytic efficiencyComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationSupplementary data010405 organic chemistryNucleotides[CHIM.CATA]Chemical Sciences/CatalysisDNADNA Catalytic0104 chemical sciences[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsG-QuadruplexesCatalytic cyclechemistryBiochemistryPeroxidasesSynthetic Biology and ChemistryHeminOverall efficiencyHeminNucleic Acids Research
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The shell-forming proteome of Lottia gigantea reveals both deep conservations and lineage-specific novelties

2013

19 pages; International audience; Proteins that are occluded within the molluscan shell, the so-called shell matrix proteins (SMPs), are an assemblage of biomolecules attractive to study for several reasons. They increase the fracture resistance of the shell by several orders of magnitude, determine the polymorph of CaCO(3) deposited, and regulate crystal nucleation, growth initiation and termination. In addition, they are thought to control the shell microstructures. Understanding how these proteins have evolved is also likely to provide deep insight into events that supported the diversification and expansion of metazoan life during the Cambrian radiation 543 million years ago. Here, we p…

Glycoside Hydrolasesmedicine.medical_treatmentproteomeGastropodaMolecular Sequence DataBiologyBiochemistrymollusc shell matrix proteinsTranscriptomeCyclophilins03 medical and health sciencesPaleontologyLineage specificAnimal ShellsSequence Analysis ProteinTandem Mass Spectrometry[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionmedicineAnimalsAmino Acid Sequence14. Life underwaterMantle (mollusc)[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyCarbonic Anhydrases030304 developmental biologyExtracellular Matrix Proteins0303 health sciencesProteaseEpidermal Growth FactorSequence Homology Amino AcidLimpet030302 biochemistry & molecular biologyCell Biologybiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsbiomineralizationPeptide FragmentsProtein Structure TertiaryPeroxidasesEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeLottia giganteaElectrophoresis Polyacrylamide GelmantleBiomineralization
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Redox intermediates of plant and mammalian peroxidases: a comparative transient-kinetic study of their reactivity toward indole derivatives.

2002

Abstract A comparative study on the reactivity of five indole derivatives (tryptamine, N-acetyltryptamine, tryptophan, melatonin, and serotonin), with the redox intermediates compound I (k2) and compound II (k3) of the plant enzyme horseradish peroxidase (HRP) and the two mammalian enzymes lactoperoxidase (LPO) and myeloperoxidase (MPO), was performed using the sequential-mixing stopped-flow technique. The calculated bimolecular rate constants (k2, k3) revealed substantial differences regarding the oxidizability of the substrates by redox intermediates at pH 7.0 and 25°C. With HRP it was shown that k2 and k3 are mainly determined by the reduction potential (E°′) of the substrate with k2 bei…

Indole testTryptamineMammalsIndolesbiologyStereochemistryLactoperoxidaseBiophysicsTryptophanSubstrate (chemistry)PlantsBiochemistryHorseradish peroxidaseRedoxchemistry.chemical_compoundKineticschemistryPeroxidasesbiology.proteinAnimalsLactoperoxidaseMolecular BiologyOxidation-ReductionHorseradish PeroxidasePeroxidaseArchives of biochemistry and biophysics
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Ciona intestinalis peroxinectin is a novel component of the peroxidase–cyclooxygenase gene superfamily upregulated by LPS

2013

Peroxinectins function as hemoperoxidase and cell adhesion factor involved in invertebrate immune reaction. In this study, the ascidian (Ciona intestinalis) peroxinectin gene (CiPxt) and its expression during the inflammatory response have been examined. CiPxt is a new member of the peroxidase-cyclooxygenase gene superfamily that contains both the peroxidase domain and the integrin KGD (Lys-Gly-Asp) binding motif. A phylogenetic tree showed that CiPxt is very close to the chordate group and appears to be the outgroup of mammalian MPO, EPO and TPO clades. The CiPxt molecular structure model resulted superimposable to the human myeloperoxidase. The CiPxt mRNA expression is upregulated by LPS …

LipopolysaccharidesModels MolecularHemocytesLPSAmino Acid MotifsMolecular Sequence DataPeroxinectinImmunologyIntegrinSettore BIO/05 - ZoologiaChordatePeroxinectin;Peroxidase;Inflammation;LPS;Ciona intestinalisAnimalsCiona intestinalisAmino Acid SequenceRNA MessengerCell adhesionPhylogenyPeroxidaseInflammationRegulation of gene expressionSequence Homology Amino AcidbiologyCell adhesion moleculeAnimal Structuresbiology.organism_classificationMolecular biologyImmunity InnateProtein Structure TertiaryCiona intestinalisGene Expression RegulationPeroxidasesOrgan SpecificityMyeloperoxidaseembryonic structuresImmunologybiology.proteinCell Adhesion MoleculesDevelopmental BiologyEndostyleDevelopmental & Comparative Immunology
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Effects of inhaled glaucine on pulmonary responses to antigen in sensitized guinea pigs.

2000

The alkaloid (S)-(+)-1,2,9,10-tetramethoxyaporphine (glaucine) is a phosphodiesterase 4 inhibitor with bronchodilator and anti-inflammatory activity in vitro. In this study, we examined the in vivo effects of glaucine on an animal model of asthma. In ovalbumin sensitized guinea pigs, inhaled glaucine (10 mg ml(-1), 3 min) inhibited the acute bronchoconstriction produced by aerosol antigen (antigen response was 256+/-42 and 95+/-14 cm H(2)O l(-1) s(-1) in control and glaucine-treated animals, respectively; P<0.05). Pretreatment with glaucine (10 mg ml(-1), 10 min inhalation, 30 min pre- and 3 h post-antigen exposure) markedly reduced airway hyperreactivity to histamine, eosinophil lung accum…

MalePulmonary CirculationAporphinesEosinophil Peroxidasemedicine.drug_classBronchoconstrictionGuinea PigsPharmacologyGuinea pigCapillary Permeabilitychemistry.chemical_compoundBronchodilatormedicineCyclic AMPAnimalsAntigensLungPharmacologybiologyInhalationDose-Response Relationship Drugbusiness.industryrespiratory systemEosinophilGlaucineCyclic Nucleotide Phosphodiesterases Type 4EosinophilsTracheamedicine.anatomical_structurechemistryPeroxidases3'5'-Cyclic-AMP PhosphodiesterasesImmunologybiology.proteinBronchoconstrictionVascular Resistancemedicine.symptomBronchial HyperreactivitybusinessEosinophil peroxidaseHistamineHistamineEuropean journal of pharmacology
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Decreased level of cardiac antioxidants in endurance-trained rats.

1989

Han-Wistar rats were exposed to a 194-200 h swimming protocol which caused a significant increase in the cardiac weight. The levels of various tissue antioxidants were assayed from the myocardium of the right ventricle and from the left ventricle (subendo- and subepimyocardium). This endurance training decreased the activities of catalase in the right ventricle and in the subendo- and subepimyocardium and Cu,Zn-superoxide dismutase in the subendomyocardium as well as the concentration of vitamin E in the right ventricle and in the subendomyocardium. Also, the activity of thioredoxin reductase decreased in each part of myocardium and that of glutathione reductase in the right ventricle and i…

Malemedicine.medical_specialtyAntioxidantPhysiologymedicine.medical_treatmentGlutathione reductasePhysical ExertionAntioxidantsEndurance trainingInternal medicinemedicineAnimalsSwimmingchemistry.chemical_classificationbiologyGlutathione peroxidaseVitamin EMyocardiumRats Inbred StrainsDipeptidesRatsmedicine.anatomical_structureEndocrinologychemistryPeroxidasesVentricleCatalaseCirculatory systembiology.proteinPhysical EnduranceOxidoreductasesActa physiologica Scandinavica
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