Search results for "Oxidoreductases"

showing 10 items of 230 documents

Coexistence of thrombophilic gene polymorphisms among 559 unrelated consecutive patients with a history of thrombosis.

2001

AdultMalemedicine.medical_specialtyBiologyGastroenterologyGenetic determinismPolymorphism (computer science)Risk FactorsInternal medicineFactor V LeidenmedicineHumansThrombophiliaGeneMethylenetetrahydrofolate Reductase (NADPH2)GeneticsVenous ThrombosisOxidoreductases Acting on CH-NH Group DonorsPolymorphism GeneticVascular diseaseFactor VThrombosisHematologyMiddle Agedmedicine.diseaseThrombosisCase-Control StudiesFemaleProthrombinThrombosis research
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Lipid metabolism during exercise I: Physiological and biochemical characterization of normal healthy male subjects in relation to their physical fitn…

1978

On the basis of maximal oxygen uptake (\(\dot V\)O2 max) 18 normal, healthy men were divided into two groups of equal size: moderately trained subjects (MTR) each having \(\dot V\)O2 max below 65.0 ml·min−1·kg−1 body weight (54.0±8.3) and well trained subjects (WTR), whose \(\dot V\)O2 max exceeded 65.0 ml·min−1·kg−1 body weight (69.2±4.1). The WTR group had slightly (non significant, n.s.) higher percentage of slow twitch, oxidative (SO) fibers in M. vastus lateralis and higher (n.s.) activities of cytochrome c oxidase (CytOx), succinate dehydrogenase (SDH), 3-hydroxyacyl-CoA-dehydrogenase (HADH), and citrate synthase (CS), while lactate dehydrogenase (LDH) activity was lower (n.s.). In th…

AdultMalemedicine.medical_specialtyPhysiologyPhysical fitnessCitrate (si)-SynthaseOxidative phosphorylationBiologyModels BiologicalElectron Transport Complex IVchemistry.chemical_compoundOxygen ConsumptionPhysiology (medical)Internal medicineLactate dehydrogenasemedicineHumansCytochrome c oxidaseCitrate synthaseOrthopedics and Sports MedicineL-Lactate Dehydrogenasebusiness.industryMusclesSuccinate dehydrogenasePublic Health Environmental and Occupational Health3-Hydroxyacyl CoA DehydrogenasesOxo-Acid-LyasesVO2 maxGeneral MedicineSuccinate DehydrogenaseEndocrinologyBiochemistrychemistryPhysical Fitnessbiology.proteinLean body massOxidoreductasesbusinessEuropean Journal of Applied Physiology and Occupational Physiology
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Enzyme activities and glycogen concentration in skeletal muscle in alcoholism. The effect of abstinence and physical conditioning.

1974

. Muscle metabolism of chronic alcoholics has been studied using a muscle biopsy technique immediately after a drinking period, after 6–7 days' abstinence and after one month's physical conditioning. The activities of CPK, HK, LDH, MDH and SDH were significantly decreased in musculus vastus lateralis for 1–2 days after an alcoholic debauch. The enzyme activities of the alcoholics, who either had been abstinent for 6–7 days or in addition conditioned for one month, did not differ from those of the controls. The concentration of muscle glycogen was at the same level in both groups, but in bicycle ergometer work of an equal relative intensity the alcoholics used more glycogen than the control …

AdultMalemedicine.medical_specialtyTime Factorsmedia_common.quotation_subjectPhysical fitnessPhysical Exertionchemistry.chemical_compoundMalate DehydrogenaseInternal medicineHexokinaseInternal MedicinemedicineHumansCreatine Kinasemedia_commonchemistry.chemical_classificationMuscle biopsyPhysical Education and TrainingPhysical conditioningGlycogenmedicine.diagnostic_testL-Lactate Dehydrogenasebusiness.industryMusclesBiopsy NeedlePhosphotransferasesSkeletal muscleAbstinenceMiddle AgedSuccinate DehydrogenaseAlcohol OxidoreductasesAlcoholismEndocrinologyEnzymemedicine.anatomical_structurechemistryConditioningbusinessEnergy MetabolismGlycogenActa medica Scandinavica
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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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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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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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