Search results for "Globin"

showing 10 items of 734 documents

Interspecies comparison of neuroglobin, cytoglobin and myoglobin: Sequence evolution and candidate regulatory elements

2003

Neuroglobin and cytoglobin are two novel members of the vertebrate globin family. Their physiological role is poorly understood, although both proteins bind oxygen reversibly and may be involved in cellular oxygen homeostasis. Here we investigate the selective constraints on coding and non-coding sequences of the neuroglobin and cytoglobin genes in human, mouse, rat and fish. Neuroglobin and cytoglobin are highly conserved, displaying very low levels of non-synonymous nucleotide substitutions. An oxygen supply function predicts distinct modes of gene regulation, involving hypoxia-responsive transcription factors. To detect conserved candidate regulatory elements, we compared the neuroglobin…

Molecular Sequence DataNeuroglobinNerve Tissue ProteinsSequence alignmentRegulatory Sequences Nucleic AcidBiologyMiceSpecies SpecificityGeneticsAnimalsHumansGlobinMolecular BiologyGeneGenetics (clinical)MammalsGeneticsRegulation of gene expressionBinding SitesBase SequenceMyoglobinCytoglobinFishesDNAMRNA stabilizationBiological EvolutionGlobinsRatsOxygenGene Expression RegulationRegulatory sequenceNeuroglobinSequence AlignmentTranscription FactorsCytogenetic and Genome Research
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Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera).

2012

Abstract While O 2 -binding hemoglobin-like proteins are present in many insects, prominent amounts of hemoglobin have only been found in a few species. Backswimmers of the genera Anisops and Buenoa (Notonectidae) have high concentrations of hemoglobin in the large tracheal cells of the abdomen. Oxygen from the hemoglobin is delivered to a gas bubble and controls the buoyant density, which enables the bugs to maintain their position without swimming and to remain stationary in the mid-water zone where they hunt for prey. We have obtained the cDNA sequences of three Anisops deanei hemoglobin chains by RT-PCR and RACE techniques. The deduced amino acid sequences show an unusual insertion of a…

Molecular Sequence DataNotonectidaeLigandsBiochemistrylaw.inventionHemipteraHemoglobinslawComplementary DNAAnimalsHumansGlobinAmino Acid SequenceMolecular BiologyPhylogenychemistry.chemical_classificationbiologyHeteropteraSequence Analysis DNAbiology.organism_classificationHemipteraBiological EvolutionAmino acidOxygenKineticschemistryBiochemistryInsect ScienceRecombinant DNAInsect ProteinsHemoglobinInsect biochemistry and molecular biology
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The hemoglobin genes of Drosophila

2006

We recently reported the unprecedented occurrence of a hemoglobin gene (glob1) in the fruitfly Drosophila melanogaster. Here we investigate the structure and evolution of the glob1 gene in other Drosophila species. We cloned and sequenced glob1 genes and cDNA from D. pseudoobscura and D. virilis, and identified the glob1 gene sequences of D. simulans, D. yakuba, D. erecta, D. ananassae, D. mojavensis and D. grimshawi in the databases. Gene structure (introns in helix positions D7.0 and G7.0), gene synteny and sequence of glob1 are highly conserved, with high ds/dn ratios indicating strong purifying selection. The data suggest an important role of the glob1 protein in Drosophila, which may b…

Molecular Sequence DataSequence alignmentBiologyBiochemistryConserved sequenceEvolution MolecularHemoglobinsDrosophilidaeAnimalsDrosophila ProteinsGuanine Nucleotide Exchange FactorsAmino Acid SequenceGlobinCloning MolecularMolecular BiologyGeneConserved SequencePhylogenySyntenyGeneticsSequence Homology Amino AcidfungiIntronCell Biologybiology.organism_classificationDrosophilaDrosophila melanogasterSequence AlignmentFEBS Journal
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Distribution of Cytoglobin in the Mouse Brain

2016

Cytoglobin (Cygb) is a vertebrate globin with so far poorly defined function. It is expressed in the fibroblast cell-lineage but has also been found in neurons. Here we provide, using immunohistochemistry, a detailed study on the distribution of Cygb in the mouse brain. While Cygb is a cytoplasmic protein in active cells of the supportive tissue, in neurons it is located in the cytoplasm and the nucleus. We found the expression of Cygb in all brain regions, although only a fraction of the neurons was Cygb-positive. Signals were of different intensity ranging from faint to very intense. Telencephalic neurons in all laminae of the cerebral cortex (CCo), in the olfactory bulb (in particular pe…

Mouseneuroanatomyglobin610 MedizinNeuroscience (miscellaneous)Braincytoglobinimmunofluorescence microscopylcsh:Human anatomylcsh:RC321-571lcsh:QM1-695Cellular and Molecular Neurosciencenervous system610 Medical sciencesmouse brainAnatomyimmunofluorescencelcsh:Neurosciences. Biological psychiatry. NeuropsychiatryOriginal ResearchNeuroscienceFrontiers in Neuroanatomy
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Photon scattering as a probe of microviscosity and channel size in gels such as sickle haemoglobin.

1983

The aggregation of sickle-cell haemoglobin (HbS) is one of the most physiologically important and widely studied macromolecular gelation processes. Both the thermodynamics and kinetics of the process are important in determining the pathological consequences of deoxygenation of the red cells (and both must be understood if a rational strategy is to be developed for pharmacological intervention). We describe here a new and versatile technique for the study of the structure and formation of the HbS aggregates, that should be widely applicable to gel systems generally. We use laser autocorrelation spectroscopy to observe the diffusion of monodisperse polystyrene latex spheres in the interstice…

MultidisciplinaryChemical PhenomenaScatteringChemistryChemistry PhysicalProtein ConformationViscosityDiffusionLasersKineticsDispersityHemoglobin SickleMicrospheresMicroviscosityDiffusionKineticsBiophysicsPhysical chemistryHumansScattering RadiationSpectroscopyDeoxygenationGelsMacromoleculeProtein BindingNature
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The role of water in hemoglobin function and stability

1993

MultidisciplinaryChemistryAllosteric regulationThermodynamicsChemical stabilityHemoglobinStability (probability)Function (biology)
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l-Carnitine l-tartrate supplementation favorably affects biochemical markers of recovery from physical exertion in middle-aged men and women.

2009

The purpose of this study was to examine the effects of Carnipure tartrate (Lonza, Allendale, NJ) supplementation (total dose of 2 g/d of l-carnitine) on markers of performance and recovery from physical exertion in middle-aged men and women. Normally active and healthy men (n = 9, 45.4 +/- 5.3 years old) and women (n = 9, 51.9 +/- 5.0 years old) volunteered to participate in the investigation. Double-blind, placebo, balanced treatment presentation and crossover design were used with 3 weeks and 3 days of supplementation followed by a 1-week washout period before the other counterbalanced treatment was initiated. After 3 weeks of each supplementation protocol, each participant then performe…

Muscle tissueAdultMalemedicine.medical_specialtyXanthine OxidaseFree RadicalsEndocrinology Diabetes and MetabolismPhysical ExertionPlaceboEndocrinologyDouble-Blind MethodInternal medicineCarnitinemedicineHumansCarnitineExertionLactic AcidLeg pressTartratesCross-Over Studiesbiologybusiness.industryMyoglobinMiddle AgedCrossover studyMiddle agemedicine.anatomical_structureEndocrinologyPurinesDietary Supplementsbiology.proteinCreatine kinaseFemalebusinessBiomarkersmedicine.drugMetabolism: clinical and experimental
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New insight into the haemoglobin superfamily: preliminary crystallographic characterization of human cytoglobin.

2003

Human cytoglobin, present in almost all tissue types, is a newly identified member of the Hb superfamily. A double mutant, having both cysteines replaced by serines, has been overexpressed in Escherichia coli, purified and crystallized. A highly redundant SAD data set has been collected at the haem Fe-atom absorption edge (lambda = 1.720 A) to 2.60 A resolution. The crystals belong to the orthorhombic P2(1)2(1)2(1) space group, with unit-cell parameters a = 46.8, b = 73.1, c = 98.9 A and two molecules per asymmetric unit. The anomalous difference Patterson map clearly reveals the position of the haem Fe-atom sites, thus paving the way for SAD structure determination.

MutationBinding SitesMolecular StructureIronCytoglobinResolution (electron density)CytoglobinMutation MissenseGeneral MedicineBiologyCrystallography X-Raymedicine.disease_causeGlobinsCrystallographyStructural BiologymedicineHumansMoleculeOrthorhombic crystal systemGlobinBinding siteCrystallizationEscherichia coli
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Different relaxations in myoglobin after photolysis

2004

To clarify the interplay of kinetic hole-burning (KHB), structural relaxation, and ligand migration in myoglobin (Mb), we measured time-resolved absorption spectra in the Soret region after photolysis of carbon monoxide Mb (MbCO) in the temperature interval 120-260 K and in the time window 350 ns to 200 ms. The spectral contributions of both photolyzed (Mb * ) and liganded Mb (MbCO) have been analyzed by taking into account homogeneous bandwidth, coupling to vibrational modes, and static conformational heterogeneity. We succeeded in separating the “time-dependent” spectral changes, and this work provides possibilities to identify the events in the process of ligand rebinding. KHB is domina…

Myoglobin Molecular Dynamics Simulation active siteAbsorption spectroscopyKineticsAnalytical chemistryThermodynamicsIn Vitro TechniquesKinetic energyLigandschemistry.chemical_compoundAnimalsMultidisciplinaryBinding SitesPhotolysisLigandMyoglobinPhotodissociationTemperatureWhalesBiological SciencesKineticsMyoglobinchemistrySpectrophotometryMolecular vibrationThermodynamicsCarbon monoxide
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Spectral broadening of the Soret band in myoglobin: an interpretation by the full spectrum of low-frequency modes from a normal modes analysis.

2005

In this work the temperature dependence of the Soret band line shape in carbon-monoxy myoglobin is re-analyzed by using both the full correlator approach in the time domain and the frequency domain approach. The new analyses exploit the full density of vibrational states of carbon-monoxy myoglobin available from normal modes analysis, and avoid the artificial division of the entire set of vibrational modes coupled to the Soret transition into "high-frequency" and "low-frequency" subsets; the frequency domain analysis, however, makes use of the so-called short-times approximation, while the time domain one avoids it. Time domain and frequency domain analyses give very similar results, thus s…

Myoglobin Molecular Dynamics Simulation active siteChemistryMyoglobinSpectrum AnalysisAnharmonicityBiophysicsAnalytical chemistryTemperatureGeneral MedicineMolecular physicsVibrationSpectral lineModels ChemicalNormal modeMolecular vibrationFrequency domainComputer SimulationTime domainHarmonic oscillatorDoppler broadeningEuropean biophysics journal : EBJ
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