Search results for "Methemoglobin"

showing 5 items of 15 documents

Determination of methemoglobin in human blood after ionising radiation by EPR

2015

In the present work presents results of investigations of radiation influence on blood of patients examined by radio-isotopes diagnosis (Tc 99m ), blood of Chernobyl clean-up workers and human blood irradiated by LINAC using Electron Paramagnetic Resonance (EPR). The EPR spectroscopy reveals information on electronic states of transition metal ions, particularly Fe 3+ in different spin states. It is shown that EPR spectra of blood of patients before examination has signal from metal-protein transferrin (g=4.3) and after administration of radio- isotope proves signal of Fe 3+ (methemaglobin) in the high spin state (g=6.0). The EPR spectra of Chernobyl liquidator display number of signals inc…

Nuclear magnetic resonanceIsotopeSpin statesChemistrylawAnalytical chemistryIrradiationElectron paramagnetic resonanceSpectral lineMethemoglobinIonizing radiationIonlaw.inventionIOP Conference Series: Materials Science and Engineering
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Oxidized respiratory molecules induced in vivo by nitrite in Pontodrilus littoralis (oligochaeta)

1992

Abstract 1. The in vivo effect of nitrite has been investigated in Pontodrilus littoralis. 2. Exposure of the animals at nitrite concentrations (0.05–0.1%) produced methaemoglobin and hemichromes. 3. Disappearance of oxidized forms was obtained when normal rearing conditions were restored. 4. Longer exposure to higher nitrite concentrations produced irreversible oxidized forms.

PharmacologyHemeproteinImmunologychemistry.chemical_elementNitrogenMethemoglobinchemistry.chemical_compoundBiochemistrychemistryIn vivoToxicityHemoglobinRespiratory systemNitriteComparative Biochemistry and Physiology Part C: Comparative Pharmacology
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Unveiling the timescale of the R-T transition in human hemoglobin.

2010

Time-resolved wide-angle X-ray scattering, a recently developed technique allowing to probe global structural changes of proteins in solution, was used to investigate the kinetics of R-T quaternary transition in human hemoglobin and to systematically compare it to that obtained with time-resolved optical spectroscopy under nearly identical experimental conditions. Our data reveal that the main structural rearrangement associated with the R-T transition takes place approximately 2 mus after the photolysis of hemoglobin at room temperature and neutral pH. This finding suggests that the 20-mus step observed with time-resolved optical spectroscopy corresponds to a small and localized structural…

PhotochemistryProtein ConformationKineticsMethemoglobinHemoglobinsStructural BiologyHumansScattering RadiationSpectroscopyMolecular BiologyallosteryScatteringChemistryProtein dynamicsSpectrum AnalysisPhotodissociationhemoglobinHydrogen-Ion ConcentrationSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CrystallographyKineticsStructural changeChemical physicshemoglobin; allostery; protein dynamicsprotein dynamicssense organsHemoglobinJournal of molecular biology
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Odd haemoglobins in odd-toed ungulates: Impact of selected haemoglobin characteristics of the white rhinoceros (Ceratotherium simum) on the monitorin…

2019

Background Due to the current poaching crisis in Africa, increasing numbers of white rhinoceroses (Ceratotherium simum) require opioid immobilisation for medical interventions or management procedures. Alarmingly, the results of both blood gas analysis and pulse oximetry regularly indicate severe hypoxaemia. Yet, the recovery of the animals is uneventful. Thus, neither of the techniques seems to represent the real oxygenation level. We hypothesized that unusual haemoglobin characteristics of this species interfere with the techniques developed and calibrated for the use in human patients. Methods Haemoglobin was isolated from blood samples of four adult, white rhinoceroses. Oxygen dissociat…

PhysiologyOxygenMethemoglobinAnalytical Chemistry0403 veterinary scienceHemoglobins0302 clinical medicineHigh oxygenMedicine and Health SciencesOximetryMammalsAnalgesicsMultidisciplinarybiologymedicine.diagnostic_testCeratotherium simumApplied MathematicsSimulation and ModelingQChemical ReactionsREukaryotaDrugs04 agricultural and veterinary sciencesHydrogen-Ion ConcentrationBody FluidsAnalgesics OpioidChemistryBloodSpectrophotometryPhysical SciencesVertebratesMedicineAnatomyAlgorithmsResearch ArticleChemical ElementsChemical Dissociation040301 veterinary sciencesAnimal TypesScienceEquineschemistry.chemical_elementRhinocerosResearch and Analysis MethodsAbsorbance03 medical and health sciencesChemical AnalysismedicineAnimalsHumansPain ManagementGas AnalysisDomestic AnimalsHorsesPerissodactylaPharmacologyChromatographyOrganismsBiology and Life SciencesOxygenationbiology.organism_classificationOxygenOpioidsPulse oximetry030228 respiratory systemchemistryAfricaAmniotesBlood Gas AnalysisZoologyMathematicsPLoS ONE
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<title>Micro-Raman scattering and infrared spectra of hemoglobin</title>

2008

Confocal micro-Raman and FT-IR spectroscopies have been used for detection of radiation influence of hemoglobin of patients examined by radio-isotopes diagnosis (Tc99m). After irradiation we observed some little changes of the Raman scattering bands which connected with out of plane porphyrine bending vibrations, also we observed additional band due to methemoglobin. Radiation of blood lead to the transition from hemoglobin (Fe2+) to methemoglobin (Fe3+) with a delocalization of iron from porphyrine plane. It was shown that FT-IR spectra indicate the radiation effects on hemoglobin.© (2008) COPYRIGHT SPIE--The International Society for Optical Engineering. Downloading of the abstract is per…

inorganic chemicalsScatteringChemistryAnalytical chemistryInfrared spectroscopyMethemoglobinSpectral lineFourier transform spectroscopysymbols.namesakeNuclear magnetic resonancesymbolsIrradiationHemoglobinRaman scatteringSPIE Proceedings
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