Search results for "Hemoglobin"

showing 10 items of 504 documents

Snapshot RGB mapping of skin melanin and hemoglobin.

2015

The concept of snapshot red-green-blue (RGB) multispectral imaging was applied for skin chromophore mapping. Three monochromatic spectral images have been extracted from a single RGB image dataset at simultaneous illumination of skin by 473-, 532-, and 659-nm laser lines. The spectral images were further transformed into distribution maps of skin melanin, oxyhemoglobin, and deoxyhemoglobin, related to pigmented and vascular skin malformations. The performance and clinical potential of the proposed technique are discussed

Materials scienceMultispectral imageBiomedical EngineeringImage processingDermoscopySensitivity and SpecificitySkin DiseasesBiomaterialsMelaninHemoglobinsOpticsHumansComputer visionTissue DistributionImage sensorSkinMelaninsintegumentary systembusiness.industryReproducibility of ResultsImage segmentationAtomic and Molecular Physics and OpticsElectronic Optical and Magnetic MaterialsMolecular ImagingRGB color modelSnapshot (computer storage)ColorimetryMonochromatic colorArtificial intelligencebusinessBiomarkersJournal of biomedical optics
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Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

2008

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.

Materials scienceProtein ConformationCrystallography X-RayBiochemistrySensitivity and SpecificityArticlechemistry.chemical_compoundHemoglobinsProtein structureScattering RadiationSpectroscopyWide-angle X-ray scatteringMolecular Biologyprotein dynamics conformational changes hemoglobin myoglobin cytochrome cScatteringMyoglobinX-RaysResolution (electron density)Cytochromes cCell BiologyNanosecondMyoglobinchemistryChemical physicsProtein quaternary structuresense organsBiotechnology
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Aptamer-embedded DNA origami cage for detecting (glycated) hemoglobin with a surface plasmon resonance sensor

2020

DNA origami-based cages functionalized with aptamer motifs, were used to detect hemoglobin and glycated hemoglobin. The binding between the cages and hemoglobin was monitored using a surface plasmon resonance (SPR) sensor. One DNA strand in the nano-cage was replaced with an aptamer that demonstrated a high affinity to hemoglobin (Hb) or glycated hemoglobin (gHb). Three types of the DNA nano-cages designed to fit the size and shape of hemoglobin were evaluated: one without an aptamer, one with the Hb-affinity aptamer (HA) and one with the gHb-affinity aptamer (GHA). Both DNA nano-cages embedded with HA and GHA showed significantly more stable binding with Hb and gHb by 5 and 9 times, respec…

Materials scienceSurface plasmon resonance sensorAptamerAptamerDissociation constant02 engineering and technologybiosensorit010402 general chemistry01 natural sciencesSurface plasmon resonance sensorchemistry.chemical_compoundGlycated hemoglobinnanorakenteethemoglobiiniDNA origamiGeneral Materials ScienceSurface plasmon resonanceMechanical EngineeringDNA021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesplasmonitDissociation constantchemistryMechanics of MaterialsBiophysicsDNA origamiHemoglobinGlycated hemoglobin0210 nano-technologyDNAMaterials Letters
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RGB imaging system for mapping and monitoring of hemoglobin distribution in skin

2011

A prototype R-G-B imaging system for mapping of skin hemoglobin distribution has been designed and tested. Device basically consists of a commercial RGB sensor (CMOS, max. frame rate 87 fps for VGA resolution), RGB LED ringlight illuminator and orthogonally orientated polarizers for reducing specular reflectance. The system was examined for monitoring of hemoglobin concentration changes during specific provocations - arterial/venous occlusions and heat test. Hemoglobin distribution maps of several skin malformations were obtained, as well.

Materials scienceVideo Graphics Arraybusiness.industryPolarizerFrame rateReflectivitylaw.inventionOpticslawRGB color modelComputer visionHemoglobinSpecular reflectionArtificial intelligencebusinessSPIE Proceedings
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OXYGEN SOLUBILITY IN NORMAL HUMAN BLOOD

1981

Publisher Summary This chapter describes oxygen solubility in normal human blood. The most crucial problem in measuring physically dissolved oxygen in blood is the prevention of oxygen binding by hemoglobin (Hb). The chapter discusses a study for the re-determination of oxygen solubility in untreated human blood. The oxygen concentration was measured by a photometric method and the Hb-concentration was determined by the cyanohemoglobin method. Oxygen solubility in normal and untreated blood is a linear function of the Hb-concentration. Hemoglobin in the reduced state has a greater influence on oxygen solubility than hemoglobin. Red cell membranes have no measureable effect on the oxygen sol…

MembraneChromatographyRed CellHuman bloodChemistryLimiting oxygen concentrationHemoglobinCyanohemoglobinOxygen solubilityOxygen binding
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Diagnostic use of fructosamine assay in the control of type II diabetes mellitus.

1988

In an attempt to evaluate the usefulness of fructosamine assay in monitoring type II diabetes, 142 diabetic patients were investigated. Fructosamine values were found to be higher in patients on insulin treatment than on oral hypoglycemic agents. In order to evaluate the metabolic control by using the correlated variations of F, Gm and HbAlc, the patients were subdivided into many control classes: mean values of fructosamine were higher in poorly controlled patients. Fructosamine however correlated better with glycemia in patients with recent variations in metabolic state than HbAlc. It was concluded that fructosamine is a good index for short-term metabolic control, and if used in an integ…

Metabolic stateAdultBlood GlucoseMalemedicine.medical_specialtyEndocrinology Diabetes and Metabolismmedicine.medical_treatmentGastroenterologyType ii diabeteschemistry.chemical_compoundEndocrinologyPhenforminReference ValuesDiabetes mellitusInternal medicineGlyburideInternal MedicineMedicineHumansInsulinIn patientGlycated Hemoglobinbusiness.industryInsulinHexosaminesGeneral MedicineMiddle Agedmedicine.diseaseFructosamineEndocrinologychemistryDiabetes Mellitus Type 2Metabolic control analysisOral hypoglycemic agentsFructosamineFemalebusinessActa diabetologica latina
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Hemocyanin from E. californicum encapsulated in silica gels: oxygen binding and conformational states.

2007

Cooperativity depends on the existence of equilibria among functionally distinct conformational states that are affected by homo and heterotropic effectors. In order to isolate the quaternary conformations of hemocyanin from E. californicum, the 24-meric giant protein was encapsulated in wet, nanoporous silica gels, either in the absence or presence of oxygen. The deoxy- and oxy-hemocyanin gels exhibit a p50 for oxygen of 11 and 2.5 torr, respectively, values in close agreement with those for hemocyanin in solution. The observed Hill coefficients are lower than unity, indicating a conformational heterogeneity within each locked conformational state, a finding in agreement with the assumptio…

Models MolecularAbsorption spectroscopyProtein Conformationmedicine.medical_treatmentchemistry.chemical_elementCooperativityBiologyOxygenGeneticsmedicineAnimalsNanoporousHemocyaninSpidersGeneral MedicineSilicon DioxideOxygenSolutionsCrystallographyKineticsBiochemistrychemistrySpectrophotometryHemocyaninsHemoglobinGelsOxygen bindingAlgorithmsProtein BindingGene
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The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin

2012

International audience; The acknowledged success of the Monod-Wyman-Changeux (MWC) allosteric model stems from its efficacy in accounting for the functional behavior of many complex proteins starting with hemoglobin (the paradigmatic case) and extending to channels and receptors. The kinetic aspects of the allosteric model, however, have been often neglected, with the exception of hemoglobin and a few other proteins where conformational relaxations can be triggered by a short and intense laser pulse, and monitored by time-resolved optical spectroscopy. Only recently the application of time-resolved wide-angle X-ray scattering (TR-WAXS), a direct structurally sensitive technique, unveiled th…

Models MolecularProtein ConformationcooperativityMESH: Catalytic DomainCooperativity01 natural sciencesMESH: Recombinant ProteinsHemoglobinsProtein structureMESH: Protein ConformationCatalytic Domainprotein structural dynamicsMESH: Allosteric Site0303 health sciencesMultidisciplinaryallosterybiologyMESH: KineticsChemistryBiological SciencesRecombinant Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMESH: HemoglobinsAllosteric SiteMESH: Models MolecularAdultMESH: MutationStereochemistryKineticsAllosteric regulation010402 general chemistry03 medical and health sciencesprotein conformational changesflash photolysisallostery; cooperativity; flash photolysis; hemoglobin; protein conformational changes; protein structural dynamics; time-resolved wide angle x ray scattering; time-resolved x-ray scatteringHumans030304 developmental biologytime-resolved X-ray scattering; protein conformational changes; cooperativity; flash photolysisMESH: Humanstime-resolved X-ray scatteringWild typeActive sitetime-resolved wide angle x ray scatteringMESH: AdulthemoglobinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesprotein conformational changeKineticsAllosteric enzymeMutationbiology.proteinHemoglobin
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Structure of the altitude adapted hemoglobin of Guinea pig in the R2-state

2010

Background: Guinea pigs are considered to be genetically adapted to a high altitude environment based on the consistent finding of a high oxygen affinity of their blood. Methodology/Principal Findings: The crystal structure of guinea pig hemoglobin at 1.8 A u resolution suggests that the increased oxygen affinity of guinea pig hemoglobin can be explained by two factors, namely a decreased stability of the Tstate and an increased stability of the R2-state. The destabilization of the T-state can be related to the substitution of a highly conserved proline (P44) to histidine (H44) in the a-subunit, which causes a steric hindrance with H97 of the b-subunit in the switch region. The stabilizatio…

Models MolecularSteric effectsGuinea PigsBiophysicslcsh:Medicinechemistry.chemical_elementCrystallography X-RayBiochemistryOxygen570 Life sciencesGuinea pigHemoglobinsAltitudeBiophysics/Macromolecular Assemblies and MachinesAnimalsProlineProtein Structure Quaternarylcsh:ScienceHistidineMultidisciplinaryProtein StabilityAltitudelcsh:ROxygen transportAdaptation PhysiologicalBiochemistry/Molecular EvolutionBiochemistry/Macromolecular Assemblies and MachinesBiochemistrychemistryBiophysicsPhysiology/Respiratory Physiologylcsh:QHemoglobinResearch Article570 Biowissenschaften
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High Pressure Enhances Hexacoordination in Neuroglobin and Other Globins

2005

The techniques of high applied pressure and flash photolysis have been combined to study ligand rebinding to neuroglobin (Ngb) and tomato Hb, globins that may display a His-Fe-His hexacoordination in the absence of external ligands. High pressure induces a moderate decrease in the His association rate and a large decrease in His dissociation rate, thus leading to an enhancement of the overall His affinity. The overall structural difference between penta- and hexacoordinated globins may be rather small and can be overcome by external modifications such as high pressure. Over the pressure range 0.1-700 MPa (7 kbar), the globins may show a loss of over a factor of 100 in the amplitude of the b…

Models MolecularSteric effectsProtein ConformationStereochemistryIronNeuroglobinchemistry.chemical_elementNerve Tissue ProteinsHemeLigandsBiochemistryOxygenHemoglobinschemistry.chemical_compoundSolanum lycopersicumPressureAnimalsHumansHistidineHorsesGlobinMolecular BiologyHemeBinding SitesPhotolysisMyoglobinChemistryPhotodissociationHeartCell BiologyLigand (biochemistry)GlobinsOxygenKineticsNeuroglobinBiophysicsFlash photolysisProtein BindingJournal of Biological Chemistry
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