Search results for "Hemeprotein"

showing 10 items of 29 documents

Fasciola spp: Mapping of the MF6 epitope and antigenic analysis of the MF6p/HDM family of heme-binding proteins

2017

MF6p/FhHDM-1 is a small cationic heme-binding protein which is recognized by the monoclonal antibody (mAb) MF6, and abundantly present in parenchymal cells and secreted antigens of Fasciola hepatica. Orthologs of this protein (MF6p/HDMs) also exist in other causal agents of important foodborne trematodiasis, such as Clonorchis sinensis, Opisthorchis viverrini and Paragonimus westermani. Considering that MF6p/FhHDM-1 is relevant for heme homeostasis in Fasciola and was reported to have immunomodulatory properties, this protein is expected to be a useful target for vaccination. Thus, in this study we mapped the epitope recognized by mAb MF6 and evaluated its antigenicity in sheep. The sequenc…

0301 basic medicineParagonimus westermaniFasciola sppPhysiologyProtein ConformationFlatwormslcsh:MedicineProtein Structure PredictionBiochemistryEpitopeAntigenicEpitopes0302 clinical medicineAnimal CellsImmune PhysiologyMedicine and Health SciencesMacromolecular Structure AnalysisMF6p/HDMEnzyme-Linked Immunoassayslcsh:ScienceMammalsNeuronsImmune System ProteinsMultidisciplinaryFasciolabiologyVaccinationEukaryotaAntibodies MonoclonalRuminantsDendritic StructureVertebratesCellular TypesAntibodyResearch ArticleHemeproteinsProtein StructureAntigenicityFascioliasisHeme bindingImmunology030231 tropical medicineAntibodies HelminthEnzyme-Linked Immunosorbent AssayHemeResearch and Analysis MethodsTrematodesAntibodiesHeme-Binding Proteins03 medical and health sciencesHelminthsparasitic diseasesParasitic DiseasesFasciola hepaticaAnimalsImmunoassaysMolecular BiologySheeplcsh:ROrganismsBiology and Life SciencesProteinsCell BiologyDendritesNeuronal DendritesFasciola hepaticabiology.organism_classificationInvertebratesMolecular biologyFasciola030104 developmental biologyEpitope mappingCellular NeuroscienceAntigens HelminthAmniotesImmunologic Techniquesbiology.proteinlcsh:QCarrier ProteinsEpitope MappingNeuroscience
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Low temperature optical spectroscopy of low-spin ferric hemeproteins

1996

We report the Soret absorption spectra (500-350 nm) of the cyanomet derivatives of human hemoglobin and horse myoglobin, in the temperature range 300-20 K and in two different solvents (65% v/v glycerol-water or 65% v/v ethylene glycol-water). In order to obtain information on stereodynamic properties of active site of the two hemeproteins, we perform an analysis of the band profiles within the framework of electron-vibrations coupling. This approach enables us to single out the various contributions to the spectral bandwidth, such as those arising from non-radiative decay of the excited electronic state (homogeneous broadening) and from the coupling of the electronic transition i) with hig…

Binding SitesAbsorption spectroscopyChemistryIronBiophysicsAnalytical chemistryGeneral MedicineSoft modesAtmospheric temperature rangeSpectral lineMolecular electronic transitionCold TemperatureSpectrophotometrySolventsAnimalsHumansPhysical chemistryHorsesHemeproteinsMetmyoglobinMuscle SkeletalHomogeneous broadeningSpectroscopyOxidation-ReductionMethemoglobin
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A Versatile and Convenient Method for the Functionalization of Porphyrins

2001

International audience; The condensation of 3-(chloromethyl)benzoyl chloride with different atropisomers of meso-(tetra-o-aminophenyl)porphyrin (TAPP), followed by the reaction of a series of nucleophilic reagents leads, among others, to precursors of biomimetic models of heme proteins such as cytochrome c oxidase (CcO). This synthesis can also be applied as an efficient two-step reaction to obtain highly functionalized porphyrin derivatives potentially useful for cation binding.

Cation bindingAtropisomerHemeproteinPorphyrinsChemistryEnzyme modelsOrganic ChemistryPorphyrinCombinatorial chemistry[ CHIM ] Chemical SciencesHeme proteinschemistry.chemical_compoundBenzoyl chlorideNucleophileReagentCationspolycyclic compounds[CHIM]Chemical SciencesOrganic chemistrySurface modificationPhysical and Theoretical ChemistryOxidoreductases
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ON THE OCCURRENCE OF RESPIRATORY COMPONENTS IN RAT-LIVER NUCLEI.

1965

Summary 1. Low-temperature spectrophotometric studies have been carried out on rat-liver nuclei isolated by two different procedures. Comparison of nuclei prepared in non-aqueous media with those prepared in high-density sucrose reveals only small quantitative differences. 2. The presence of hemoglobin, cytochrome b 5 , and cytochrome c was detected in both types of nuclei. No cytochrome b , or cytochrome oxidase could be found. Studies on the possible origin of the hemoproteins suggest that hemoglobin and cytochrome b 5 are of extra-nuclear origin. The presence of cytochrome c as a nuclear component could not be ruled out completely although leakage from mitochondria was also considered a …

Cell NucleusHemeproteinCytochrome bCytochrome cResearchRespiratory chainFlavin groupDNABiologyBiochemistryRatschemistry.chemical_compoundHemoglobinsMetabolismBiochemistrychemistryLiverSpectrophotometrybiology.proteinRespiratory pigmentCytochrome c oxidaseCytochromesRNAHemoglobinBiochimica et biophysica acta
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Alkaline haematin D-575, a new tool for the determination of haemoglobin as an alternative to the cyanhaemiglobin method. I. description of the method

1984

A new method for the rapid and accurate measurement of haemoglobin has been developed as an alternative to the conventional cyanhaemiglobin method. This method is based on the conversion of all haeme, haemoglobin, and haemiglobin species into a stable end product by an alkaline solution of a non-ionic detergent ('AHD reagent'). The reaction product, designated as alkaline haematin D-575, is extremely stable and shows a characteristic absorption peak at 575 nm. As compared to the cyanhaemiglobin method, the determination of haemoglobin by alkaline haematin D-575 offers several advantages such as (1) extreme stability of the AHD reagent and the conversion product, (2) decreased conversion tim…

ChromatographyHemeproteinOctoxynolChemistryStereochemistrySmokingBiochemistry (medical)Clinical BiochemistryHemeGeneral MedicineHydrogen-Ion ConcentrationBiochemistryHaematinPolyethylene GlycolsReaction productPhotometryHemoglobinschemistry.chemical_compoundBasic solutionReagentHeminHumansHemoglobinClinica Chimica Acta
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Hemoglobin dynamics in rat erythrocytes investigated by M�ssbauer spectroscopy

1991

Rats have been enriched in 57Fe and erythrocytes were isolated from the blood. Mössbauer absorption spectroscopy on the hemoglobin of these erythrocytes has shown rather similar dynamics as found earlier in crystals of myoglobin, in frozen solutions of human hemoglobin and in a number of other proteins. The results strongly indicate that the motion of the heme and presumably some part of the F-helix is mainly influenced by the average viscosity of the sample determined by a network of hydrogen bridges and other weak interactions. Extrapolations of Mössbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins.

ErythrocytesHemeproteinAbsorption spectroscopyProtein ConformationIronProtein dynamicsBiophysicsAnalytical chemistryHemeGeneral MedicineRatsHemoglobinsKineticsSpectroscopy MossbauerRed blood cellchemistry.chemical_compoundmedicine.anatomical_structureMyoglobinchemistrymedicineBiophysicsAnimalsHemoglobinProtein crystallizationHemeEuropean Biophysics Journal
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Isolation and partial characterization of a cytochrome-o complex from chromatophores of the photosynthetic bacterium Rhodospirillum rubrum FR1.

1989

A cytochrome-o complex was isolated from chromatophores of photoheterotrophically grown Rhodospirillum rubrum FR1. The enzyme was extracted with the non-denaturating detergent taurodeoxycholate and subsequently purified by sucrose-density-gradient centrifugation and gel-permeation HPLC. The complex contains two types of cytochromes, one of them cytochrome o, and two copper atoms. It catalyzes the reduction of molecular oxygen, when N,N,N',N'-tetramethyl-p-phenylenediamine or ubiquinol 10 are offered as electron donors. The oxidase activity is inhibited by cyanide, carbon monoxide and 2-heptyl-2-hydroxyquinoline N-oxide. The molecular mass of the protein is 136 +/- 15 kDa. The subunit analys…

Gel electrophoresisOxidase testUbiquinolHemeproteinCytochromebiologyMolecular massChemistryProtein subunitEscherichia coli ProteinsRhodospirillum rubrumPhotosynthetic Reaction Center Complex ProteinsDithioniteBacterial Chromatophoresbiology.organism_classificationCytochrome b GroupBiochemistrychemistry.chemical_compoundBiochemistryBacterial Proteinsbiology.proteinCytochromesElectrophoresis Polyacrylamide GelRhodospirillumEuropean journal of biochemistry
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Nature of O2, CO, and CN binding to hemoprotein models

2004

Parametrization of a molecular-mechanics program to include terms specific for five- and six-coordinate transition metal complexes results in computer-simulated structures of hemo complexes. The principal new feature peculiar to five- and six-coordination is a term that measures the effect of electron-pair repulsion modified by the ligand electronegativity and takes into account the different structural possibilities. The work consists in the modification of program molecular mechanics for penta and hexacoordination. The model system takes into account the structural differences of the fixing center in the hemoglobin subunits. The customary proximal histidine is added. The macrocycle hemo I…

HemeproteinBent molecular geometryHemoglobin SubunitsCondensed Matter PhysicsLigand (biochemistry)PorphyrinAtomic and Molecular Physics and OpticsElectronegativitychemistry.chemical_compoundchemistryMyoglobinComputational chemistryPhysical and Theoretical ChemistryHistidineInternational Journal of Quantum Chemistry
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Erratum: Nature of O2, CO, and CN binding to hemoprotein models

2004

The original article to which this Erratum refers was published in International Journal of Quantum Chemistry (2004) 99(6)

HemeproteinChemistryComputational chemistryPhysical and Theoretical ChemistryCondensed Matter PhysicsQuantum chemistryAtomic and Molecular Physics and OpticsInternational Journal of Quantum Chemistry
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Androgen hydroxylation catalysed by a cell line (SD1) that stably expresses rat hepatic cytochrome P-450 PB-4 (IIB1).

1989

Androgen hydroxylation catalysed by Chinese hamster fibroblast SD1 cells, which stably express cytochrome P-450 form PB-4, the rat P450IIB1 gene product, was assessed and compared to that catalysed by purified cytochrome P-450 PB-4 isolated from rat liver. SD1 cell homogenates catalysed the NADPH-dependent hydroxylation of androstenedione and testosterone with a regioselectivity very similar to that purified by P-450 PB-4 (16 beta-hydroxylation/16 alpha-hydroxylation = 6.0-6.8 for androstenedione; 16 beta/16 alpha = 0.9 for testosterone). Homogenates prepared from the parental cell line V79, which does not express detectable levels of P-450 PB-4 or any other cytochrome P-450, exhibited no a…

HemeproteinCytochromemedicine.drug_classBiologyHydroxylationBiochemistryCatalysisCell LineHydroxylationchemistry.chemical_compoundCricetulusCricetinaemedicineAnimalsTestosteroneAndrostenedioneMolecular BiologyAndrostenedioneCytochrome P450Cell BiologyFibroblastsAndrogenRatsBiochemistrychemistryLiverSteroid 16-alpha-HydroxylaseCell cultureSteroid HydroxylasesMicrosomebiology.proteinSteroid 11-beta-HydroxylaseAryl Hydrocarbon HydroxylasesResearch Article
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