Search results for "Reductases"

showing 10 items of 276 documents

Anaerobic threshold, skeletal muscle enzymes and fiber composition in young female cross-country skiers.

1980

Anaerobic threshold (AT) and maximum oxygen uptake (max VO2) were determined in 15 young female cross-country skiers, aged 15--20 years, during incremental bycycle ergometer exercise. Succinate dehydrogenase (SDH), malate dehydrogenase (MDH), citrate synthase (CS) and lactate dehydrogenase (LDH) were analyzed biochemically and percentage of slow twitch fibres (%ST fibres, myosin adenosine triphosphatase staining) histochemically in muscle samples obtained from m. vastus lateralis. Max VO2 correlated significantly with anaerobic threshold in ml x kg-1 x min-1 (mlAT) but when AT was expressed in percent of max VO2 (%AT) the correlation was insignificant. Significant correlations were found be…

Adultmedicine.medical_specialtyAdolescentPhysiologyPhysical ExertionCitrate (si)-SynthaseSports MedicineMalate dehydrogenasechemistry.chemical_compoundMalate DehydrogenaseInternal medicineLactate dehydrogenaseMyosinmedicineCitrate synthaseHumansbiologyL-Lactate DehydrogenaseSuccinate dehydrogenaseMusclesRespirationSkeletal muscleVO2 maxOxo-Acid-LyasesSuccinate DehydrogenaseEndocrinologymedicine.anatomical_structureBiochemistrychemistrybiology.proteinLactatesPhysical EnduranceFemaleOxidoreductaseshuman activitiesAnaerobic exerciseActa physiologica Scandinavica
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VITAMIN K-INDUCED MODIFICATION OF COAGULATION PHENOTYPE IN VKORC1 HOMOZYGOUS DEFICIENCY

2008

Summary.  Background: Combined vitamin K-dependent clotting factor (VKCF) deficiency type 2 (VKCFD2) is a rare bleeding disorder caused by mutated vitamin K 2,3-epoxide reductase complex subunit 1 (VKORC1) gene. Methods and results: An Italian patient with moderate to severe bleeding tendency was genotyped, and found to be homozygous for the unique VKORC1 mutation (Arg98Trp) so far detected in VKCFD2. The activity levels of VKCFs were differentially reduced, and inversely related to the previously estimated affinity of procoagulant factor propeptides for the γ-carboxylase. The normal (factor IX) or reduced antigen levels (other VKCFs) produced a gradient in specific activities. Vitamin K su…

Adultmedicine.medical_specialtycoagulation factor levelsVitamin KProtein SMixed Function OxygenasesTissue factorchemistry.chemical_compoundInternal medicineVitamin K Epoxide ReductasesmedicineVKCFD2HumansFactor IXClotting factorCoagulation factor levels; Thrombin generation; Vitamin K supplementation; VKCFD2; VKORC1 mutation;biologyFactor VIIChemistryFactor XHomozygotevitamin K supplementationHematologyBlood Coagulation DisordersEndocrinologyTreatment OutcomeCoagulationthrombin generationImmunologyMutationbiology.proteinFemaleBlood Coagulation TestsVKCFD2 VKORC1 mutation coagulation factor levels thrombin generation vitamin K supplementationProtein Cmedicine.drugHalf-LifeVKORC1 mutation
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Properties of Resveratrol:In VitroandIn VivoStudies about Metabolism, Bioavailability, and Biological Effects in Animal Models and Humans

2015

Plants containing resveratrol have been used effectively in traditional medicine for over 2000 years. It can be found in some plants, fruits, and derivatives, such as red wine. Therefore, it can be administered by either consuming these natural products or intaking nutraceutical pills. Resveratrol exhibits a wide range of beneficial properties, and this may be due to its molecular structure, which endow resveratrol with the ability to bind to many biomolecules. Among these properties its activity as an anticancer agent, a platelet antiaggregation agent, and an antioxidant, as well as its antiaging, antifrailty, anti-inflammatory, antiallergenic, and so forth activities, is worth highlightin…

AgingAntioxidantendocrine system diseasesmedicine.medical_treatmentAnti-Inflammatory AgentsBiological AvailabilityAntineoplastic AgentsApoptosisReview ArticleResveratrolPharmacologyBiologyBiochemistryAntioxidantschemistry.chemical_compoundNutraceuticalPharmacokineticsIn vivoStilbenesmedicineAnimalsHumansSirtuinslcsh:QH573-671lcsh:Cytologyorganic chemicalsfood and beveragesCell BiologyGeneral MedicineMetabolismIn vitroBioavailabilitychemistryBiochemistryResveratrolModels AnimalOxidoreductasesOxidative Medicine and Cellular Longevity
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Prostaglandin D2 regulates joint inflammation and destruction in murine collagen-induced arthritis.

2012

Item does not contain fulltext OBJECTIVE: Prostaglandin D2 (PGD2) may exert proinflammatory or antiinflammatory effects in different biologic systems. Although this prostanoid and the enzymes responsible for its synthesis are up-regulated by interleukin-1beta (IL-1beta) in human chondrocytes in vitro, the role of PGD2 in arthritis remains unclear. This study was undertaken to investigate the role of PGD2 in the inflammatory response and in joint destruction during the development of collagen-induced arthritis (CIA) in mice. METHODS: PGD2 and cytokine levels in mice with CIA were determined by enzyme-linked immunosorbent assay. Expression of hematopoietic PGD synthase (h-PGDS), lipocalin-typ…

Agonistmusculoskeletal diseasesmedicine.medical_specialtyIndolesmedicine.drug_classmedicine.medical_treatmentChemokine CXCL1ImmunologyInterleukin-1betaReceptors ProstaglandinArthritisInflammationProinflammatory cytokinechemistry.chemical_compoundMiceRheumatologyBone MarrowInternal medicinemedicineImmunology and AllergyAnimalsPharmacology (medical)Receptors ImmunologicReceptorintegumentary systembusiness.industryProstaglandin D2Hydantoinsmedicine.diseaseArthritis ExperimentalLipocalinsHindlimbInterleukin-10Up-RegulationIntramolecular OxidoreductasesInterleukin 10CytokineEndocrinologychemistryMice Inbred DBACytokinesJointslipids (amino acids peptides and proteins)Prostaglandin D2Immune Regulation Auto-immunity transplantation and immunotherapy [NCMLS 2]medicine.symptombusiness
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Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications

1997

In Escherichia coli the expression of the nuo genes encoding the proton pumping NADH dehydrogenase I is stimulated by the presence of fumarate during anaerobic respiration. The regulatory sites required for the induction by fumarate, nitrate and O2 are located at positions around –309, –277, and downstream of –231 bp, respectively, relative to the transcriptional-start site. The fumarate regulator has to be different from the O2 and nitrate regulators ArcA and NarL. For growth by fumarate respiration, the presence of NADH dehydrogenase I was essential, in contrast to aerobic or nitrate respiration which used preferentially NADH dehydrogenase II. The electron transport from NADH to fumarate …

Anaerobic respirationAcetatesmedicine.disease_causeBiochemistryElectron TransportFumaratesEscherichia colimedicineDimethyl SulfoxideNADH NADPH OxidoreductasesAnaerobiosisEscherichia colichemistry.chemical_classificationElectron Transport Complex IEthanolbiologyNADH dehydrogenaseGene Expression Regulation BacterialProton PumpsElectron acceptorFumarate reductaseNADElectron transport chainGlycerol-3-phosphate dehydrogenaseBiochemistrychemistryElectron Transport Complex Ibiology.proteinEnergy MetabolismEuropean Journal of Biochemistry
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Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors

1997

AbstractThe electron-transport chains of Escherichia coli are composed of many different dehydrogenases and terminal reductases (or oxidases) which are linked by quinones (ubiquinone, menaquinone and demethylmenaquinone). Quinol:cytochrome c oxido-reductase (`bc1 complex') is not present. For various electron acceptors (O2, nitrate) and donors (formate, H2, NADH, glycerol-3-P) isoenzymes are present. The enzymes show great variability in membrane topology and energy conservation. Energy is conserved by conformational proton pumps, or by arrangement of substrate sites on opposite sides of the membrane resulting in charge separation. Depending on the enzymes and isoenzymes used, the H+/e− rat…

Anaerobic respirationTranscription GeneticCellular respirationFNRBiophysicsBiochemistryElectron TransportOxygen sensorOxygen ConsumptionBacterial Proteins(Escherichia coli)Escherichia coliProtein phosphorylationAnaerobiosischemistry.chemical_classificationbiologyCytochrome cQuinonesArcAGene Expression Regulation BacterialCell BiologyElectron acceptorElectron transport chainAerobiosisAerobic electron transportResponse regulatorAnaerobic electron transportBiochemistrychemistrybiology.proteinCarrier ProteinsEnergy MetabolismOxidoreductasesFlux (metabolism)RegulationBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Antioxidant and glutathione-related enzymatic activities in rat sciatic nerve

1990

Abstract The present work tries to establish the antioxidant capacity of the peripheral nervous tissue of the rat, in terms of the enzymatic activities present in this tissue that either prevent the formation of activated species as the semiquinone radical (DT-diaphorase), protect against activated oxygen species (superoxide dismutase, glutathione peroxidase), conjugate natural toxic products or xenobiotics (glutathione S-transferases, especially the activity conjugating 4-hydroxy-nonenal), or complete the glutathione system metabolism (glutathione disulfide reductase, γ-glutamyl transpeptidase). All the activities studied are lower in this tissue than they are in liver, except for γ-glutam…

AntioxidantGPX3medicine.medical_treatmentGlutathione reductaseToxicologyAntioxidantsSuperoxide dismutaseCellular and Molecular Neurosciencechemistry.chemical_compoundDevelopmental NeurosciencemedicineAnimalsQuinone ReductasesGlutathione Transferasechemistry.chemical_classificationGlutathione PeroxidasebiologySuperoxide DismutaseChemistryGlutathione peroxidaseNervous tissuegamma-GlutamyltransferaseGlutathioneGlutathioneSciatic NerveRatsGlutathione S-transferasemedicine.anatomical_structureBiochemistrybiology.proteinNeurotoxicology and Teratology
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Involvement of acyl coenzyme A oxidase isozymes in biotransformation of methyl ricinoleate into gamma-decalactone by Yarrowia lipolytica.

2000

ABSTRACT We reported previously on the function of acyl coenzyme A (acyl-CoA) oxidase isozymes in the yeast Yarrowia lipolytica by investigating strains disrupted in one or several acyl-CoA oxidase-encoding genes ( POX1 through POX5 ) (H. Wang et al., J. Bacteriol. 181:5140–5148, 1999). Here, these mutants were studied for lactone production. Monodisrupted strains produced similar levels of lactone as the wild-type strain (50 mg/liter) except for Δ pox3 , which produced 220 mg of γ-decalactone per liter after 24 h. The Δ pox2 Δpox3 double-disrupted strain, although slightly affected in growth, produced about 150 mg of lactone per liter, indicating that Aox2p was not essential for the biotra…

Applied Microbiology and BiotechnologyIsozymeLactonesMESH : BiotransformationBiotransformation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAcyl-CoA oxidase[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Oxidoreductases[INFO.INFO-BT]Computer Science [cs]/BiotechnologyMESH: Saccharomycetales[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyComputingMilieux_MISCELLANEOUSBiotransformationchemistry.chemical_classificationMESH : Isoenzymes[SDV.EE]Life Sciences [q-bio]/Ecology environmentMESH: BiotransformationOxidase testEcologyStrain (chemistry)biologyChemistryMESH: Acyl-CoA OxidaseYarrowiaMESH : SaccharomycetalesACYLCOENZYME Abiology.organism_classificationMESH : OxidoreductasesPhysiology and BiotechnologyYeastMESH : LactonesMESH: Ricinoleic AcidsIsoenzymes[INFO.INFO-BT] Computer Science [cs]/BiotechnologyBiochemistryMESH : Ricinoleic AcidsSaccharomycetalesMESH: IsoenzymesMESH : Acyl-CoA OxidaseAcyl-CoA OxidaseOxidoreductasesRicinoleic AcidsLactone[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: LactonesFood ScienceBiotechnology
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Energetic coupling between plastids and mitochondria drives CO2 assimilation in diatoms.

2015

International audience; Diatoms are one of the most ecologically successful classes of photosynthetic marine eukaryotes in the contemporary oceans. Over the past 30 million years, they have helped to moderate Earth's climate by absorbing carbon dioxide from the atmosphere, sequestering it via the biological carbon pump and ultimately burying organic carbon in the lithosphere. The proportion of planetary primary production by diatoms in the modern oceans is roughly equivalent to that of terrestrial rainforests. In photosynthesis, the efficient conversion of carbon dioxide into organic matter requires a tight control of the ATP/NADPH ratio which, in other photosynthetic organisms, relies prin…

Aquatic Organismschemistry.chemical_compoundAdenosine TriphosphateSettore BIO/04 - Fisiologia VegetaleCYCLIC ELECTRON FLOWPlastidsPhotosynthesisPHAEODACTYLUM-TRICORNUTUMPlant Proteinschemistry.chemical_classificationMultidisciplinarymicroalgaeRespirationCarbon fixationEnergetic interactionsProton-Motive ForceMitochondriametabolic mutantPhenotypeATP/NADPH ratioOXYGEN PHOTOREDUCTIONCarbon dioxideOxidoreductasesOxidation-ReductionOceanOceans and SeasElectron flowMarine eukaryotesBiologyPhotosynthesisCHLAMYDOMONAS-REINHARDTIICarbon cycleCarbon CycleMitochondrial ProteinsEnergetic exchangesBotanyOrganic matterEcosystem[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology14. Life underwaterPlastidEcosystemDiatomsChemiosmosisfungiECSCarbon Dioxidechemistry13. Climate actionNADP
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Disentangling the rhizosphere effect on nitrate reducers and denitrifiers: insight into the role of root exudates.

2008

International audience; To determine to which extent root-derived carbon contributes to the effects of plants on nitrate reducers and denitrifiers, four solutions containing different proportions of sugar, organic acids and amino acids mimicking maize root exudates were added daily to soil microcosms at a concentration of 150 μg C g−1 of soil. Water-amended soils were used as controls. After 1 month, the size and structure of the nitrate reducer and denitrifier communities were analysed using the narG and napA, and the nirK, nirS and nosZ genes as molecular markers respectively. Addition of artificial root exudates (ARE) did not strongly affect the structure or the density of nitrate reduce…

BACTERIAL COMMUNITY STRUCTURE REAL-TIME PCRDNA BacterialDenitrificationMolecular Sequence DataDIVERSITYBiologyGENETIC-STRUCTURENIRKNitrate reductaseMicrobiologyPlant RootsZea mays03 medical and health scienceschemistry.chemical_compoundNitrateBacterial ProteinsBotanyPLANTSSugarEcology Evolution Behavior and SystematicsNitritesSoil Microbiology030304 developmental biology2. Zero hunger0303 health sciencesRhizosphereNitratesBacteria04 agricultural and veterinary sciencesBiodiversitySequence Analysis DNA6. Clean waterCarbonSOIL[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitologychemistry13. Climate actionEnvironmental chemistrySoil water040103 agronomy & agriculture0401 agriculture forestry and fisheriesComposition (visual arts)MicrocosmOxidoreductasesOxidation-ReductionMAIZENOSZ GENESEnvironmental microbiology
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