Search results for "Escher"

showing 10 items of 728 documents

Decreasing the chlorophyll a/b ratio in reconstituted LHCII: Structural and functional consequences

1999

Trimeric (bT) and monomeric (bM) light-harvesting complex II (LHCII) with a chlorophyll a/b ratio of 0.03 were reconstituted from the apoprotein overexpressed in Escherichia coli. Chlorophyll/xanthophyll and chlorophyll/protein ratios of bT complexes and 'native' LHCII are rather similar, namely, 0.28 vs 0. 27 and 10.5 +/- 1.5 vs 12, respectively, indicating the replacement of most chlorophyll a molecules with chlorophyll b, leaving one chlorophyll a per trimeric complex. The LD spectrum of the bT complexes strongly suggests that the chlorophyll b molecules adopt orientations similar to those of the chlorophylls a that they replace. The circular dichroism (CD) spectra of bM and bT complexes…

ChlorophyllChlorophyll bProtein FoldingChlorophyll aCircular dichroismPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein Complexesmedicine.disease_causeBiochemistryAbsorptionStructure-Activity Relationshipchemistry.chemical_compoundThermolysinmedicineEscherichia colichemistry.chemical_classificationPigmentationChlorophyll ACircular DichroismCrystallographySpectrometry FluorescenceMonomerEnergy TransferchemistrySpectrophotometryChlorophyllXanthophyllBiochemistry
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A battery of toxicity tests as indicators of decontamination in composting oily waste.

2000

Heterogeneous oily waste from an old dumping site was composted in three windrows constructed from different proportions of waste, sewage sludge, and bark. The objectives of this pilot study were to examine the usefulness of composting as a treatment method for this particular waste and to study decontamination in the composting process by using a battery of toxicity tests. Five samples from the windrow having intermediate oil concentrations were tested with toxicity tests based on microbes (Pseudomonas putida growth inhibition test, ToxiChromotest, MetPLATE, and three different modifications of a luminescent bacterial test), enzyme inhibition (reverse electron transport), plants (duckweed …

ChlorophyllHealth Toxicology and MutagenesisPlant DevelopmentGerminationcomplex mixturesWindrowBioremediationPseudomonasEscherichia coliBioassayAnimalsSoil PollutantsDecontaminationSewage sludgeOrganellesPlants MedicinalEnchytraeusbiologyChemistryPublic Health Environmental and Occupational HealthFabaceaeGeneral MedicineHuman decontaminationPlantsbiology.organism_classificationPollutionInvertebratesWaste treatmentPetroleumMetalsEnvironmental chemistryToxicityLuminescent MeasurementsColorimetryDNA DamageEcotoxicology and environmental safety
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De-epoxidation of Violaxanthin in Light-harvesting Complex I Proteins

2004

The conversion of violaxanthin (Vx) to zeaxanthin (Zx) in the de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of chloroplasts against photooxidative damage. Vx is bound to the antenna proteins of both photosystems. In photosystem II, the formation of Zx is essential for the pH-dependent dissipation of excess light energy as heat. The function of Zx in photosystem I is still unclear. In this work we investigated the de-epoxidation characteristics of light-harvesting complex proteins of photosystem I (LHCI) under in vivo and in vitro conditions. Recombinant LHCI (Lhcal-4) proteins were reconstituted with Vx and lutein, and the convertibility of Vx wa…

ChlorophyllLuteinPhotosystem IIPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesXanthophyllsPhotosystem IThylakoidsBiochemistrychemistry.chemical_compoundSolanum lycopersicumSpinacia oleraceaEscherichia coliMolecular BiologyPhotosystemchemistry.chemical_classificationBinding SitesPhotosystem I Protein ComplexChemistryfood and beveragesPigments BiologicalCell Biologybeta CaroteneRecombinant ProteinsChloroplastKineticsBiochemistryXanthophyllThylakoidEpoxy CompoundsApoproteinsViolaxanthinJournal of Biological Chemistry
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Localization of the N-terminal Domain in Light-harvesting Chlorophyll a/b Protein by EPR Measurements

2005

The conformational distribution of the N-terminal domain of the major light-harvesting chlorophyll a/b protein (LHCIIb) has been characterized by electron-electron double resonance yielding distances between spin labels placed in various domains of the protein. Distance distributions involving residue 3 near the N terminus turned out to be bimodal, revealing that this domain, which is involved in regulatory functions such as balancing the energy flow through photosystems (PS) I and II, exists in at least two conformational states. Models of the conformational sub-ensembles were generated on the basis of experimental distance restraints from measurements on LHCIIb monomers and then checked f…

ChlorophyllModels MolecularThreonineConformational changeTime FactorsLightMacromolecular SubstancesProtein ConformationPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesElectronsTrimerCrystallography X-RayThylakoidsBiochemistryProtein Structure Secondarylaw.inventionResidue (chemistry)chemistry.chemical_compoundlawEscherichia coliAnimalsPhosphorylationAnnexin A4Electron paramagnetic resonanceMolecular BiologyPhotosystemPhotosystem I Protein ComplexChemistryChlorophyll AElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsProtein Structure TertiaryOxygenN-terminusCrystallographyMonomerThylakoidMutationCattleSpin LabelsDimerizationJournal of Biological Chemistry
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Cholera-Like Enterotoxins and Regulatory T cells

2010

Cholera toxin (CT) and the heat-labile enterotoxin of E. coli (LT), as well as their non toxic mutants, are potent mucosal adjuvants of immunization eliciting mucosal and systemic responses against unrelated co-administered antigens in experimental models and in humans (non toxic mutants). These enterotoxins are composed of two subunits, the A subunit, responsible for an ADP-ribosyl transferase activity and the B subunit, responsible for cell binding. Paradoxically, whereas the whole toxins have adjuvant properties, the B subunits of CT (CTB) and of LT (LTB) have been shown to induce antigen specific tolerance when administered mucosally with antigens in experimental models as well as, rece…

Cholera ToxinHealth Toxicology and Mutagenesismedicine.medical_treatmentBacterial Toxinslcsh:MedicineEnterotoxinReviewBiologyToxicologymedicine.disease_causeT-Lymphocytes Regulatoryregulatory T cellsMicrobiologyImmune toleranceAutoimmune DiseasesEnterotoxinsImmune systemAntigenAdjuvants ImmunologicmedicineImmune ToleranceAnimalsHumansAntigen-presenting cellEscherichia coli Proteinslcsh:RCholera toxinCTBIn vitroLTBImmunologyAdjuvantheat-labile enterotoxin of E. colicholera-like enterotoxinsToxins
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Biosensor-based kinetic and thermodynamic characterization of opioids interaction with human μ-opioid receptor.

2019

Development of opioid analgesics with minimal side effects requires substantial knowledge on structure-kinetic and -thermodynamic relationship of opioid-receptor interactions. Here, combined kinetics and thermodynamics of opioid agonist binding to human μ-opioid receptor (h-μOR) was investigated using real-time label-free surface plasmon resonance (SPR)-based method. The N-terminal end truncated and C-terminal 6His-tagged h-μOR was constructed and expressed in E. coli. Receptor was purified, detergent-solubilized and characterized by circular dichroism. The uniform immobilization of h-μOR on Ni-NTA chips was achieved using hybrid capture-coupling approach followed by reconstitution in lipid…

Circular dichroismThermodynamic equilibriummedicine.drug_classEnthalpyReceptors Opioid muPharmaceutical Science02 engineering and technology(+)-NaloxoneBiosensing Techniques030226 pharmacology & pharmacy03 medical and health sciences0302 clinical medicineOpioid receptormedicineEscherichia coliHumansSurface plasmon resonanceLipid bilayerMorphineChemistryNaloxone021001 nanoscience & nanotechnologyAnalgesics OpioidKineticsOpioidBiophysicsThermodynamics0210 nano-technologymedicine.drugEuropean journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences
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Cloning, purification, and nucleotide-binding traits of the catalytic subunit A of the V1VO ATPase from Aedes albopictus.

2007

The Asian tiger mosquito, Aedes albopictus, is commonly infected by the gregarine parasite Ascogregarina taiwanensis, which develops extracellularly in the midgut of infected larvae. The intracellular trophozoites are usually confined within a parasitophorous vacuole, whose acidification is generated and controlled by the V(1)V(O) ATPase. This proton pump is driven by ATP hydrolysis, catalyzed inside the major subunit A. The subunit A encoding gene of the Aedes albopictus V(1)V(O) ATPase was cloned in pET9d1-His(3) and the recombinant protein, expressed in the Escherichia coli Rosetta 2 (DE3) strain, purified by immobilized metal affinity- and ion-exchange chromatography. The purified prote…

Circular dichroismVacuolar Proton-Translocating ATPasesATPaseProtein subunitGene ExpressionGenes InsectBiologyIn Vitro Techniquesmedicine.disease_causelaw.inventionAdenosine TriphosphateATP hydrolysislawAedesCatalytic DomainmedicineAnimalsNucleotideCloning MolecularEscherichia coliDNA Primerschemistry.chemical_classificationPhotoaffinity labelingBase SequenceMolecular biologyProtein SubunitsSpectrometry FluorescenceBiochemistrychemistrySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinRecombinant DNAInsect ProteinsBiotechnologyProtein expression and purification
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Tetrahydroanthraquinone Derivatives from the Endophytic Fungus Stemphylium globuliferm

2015

Four new tetrahydroanthraquinone derivatives, namely, dihydroaltersolanol B (1), dihydroaltersolanol C (2), and the atropisomers acetylalterporriol D (3) and acetylalterporriol E (4), were obtained from the endophytic fungus Stemphylium globuliferum, which was isolated from Juncus acutus growing in Egypt. The structures of the new compounds were unambiguously elucidated on the basis of one- and two-dimensional NMR spectroscopy, as well as by high-resolution mass spectrometry and electronic circular dichroism (ECD) spectroscopy. In addition, seven known anthraquinone derivatives 5–11 were isolated and identified on the basis of their spectral characteristics and by comparison with literature…

Circular dichroismbiologyChemistryStereochemistryOrganic ChemistryNuclear magnetic resonance spectroscopymedicine.disease_causebiology.organism_classificationPlant use of endophytic fungi in defenseMinimum inhibitory concentrationStemphylium globuliferumTermészettudományokJuncus acutusmedicinePhysical and Theoretical ChemistryAntibacterial activityKémiai tudományokEscherichia coli
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An Intercalibration Study of the Use of 4-Methylumbelliferyl-β-D-Glucuronide for the Specific Enumeration of Escherichia coli in Seawater and Marine …

1991

Summary A fluorogenic assay for the specific detection of Escherichia coli on the basis of its β-glucuronidase activity (MUG method) was applied to seawater and marine sediments with different contamination levels. The study was carried out in three Mediterranean areas (Malaga-Spain, Nice-France and Palermo-Sicily), using strictly standardized methods (membrane filtration), media (mFC and Chapman-TTC agars) and reagents, to evaluate statistically its sensitivity and specificity according to the origin and contamination of samples, the workers performing the tests and the selected culture media. The results obtained indicate that the MUG method is highly specific (94.5%) and sensitive (90.8%…

Citrobacterfood.ingredientChromatographybiologyContaminationbiology.organism_classificationmedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyEnterobacteriaceaeMicrobiologyAgar platefoodmedicineAgarSeawaterEscherichia coliEcology Evolution Behavior and SystematicsBacteriaSystematic and Applied Microbiology
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Cloning and Characterization of Overlapping DNA Fragments of the Toxin A Gene of Clostridium difficile

1989

Clostridium difficile, a human pathogen, produces two very large protein toxins, A and B (250-600 kDa), which resist dissociation into subunits. To clone the toxin A gene, a genomic library of 3-8 kb chromosomal DNA fragments of C. difficile strain VPI 10463 established in pUC12 was screened with a rabbit polyclonal toxin A antiserum. Thirty-five clones were isolated which carried 2.5-7.0 kb inserts representing a 10 kb region of the C. difficile genome. All the inserts were oriented in the same direction, suggesting that toxin A gene expression was under control of the lac promoter of the pUC12 vector. Western blot experiments revealed the presence of low amounts of fusion proteins of vari…

ClostridiumDNA BacterialRecombinant Fusion ProteinsBacterial ToxinsBlotting WesternRestriction MappingClostridium difficile toxin ABiologyMolecular cloningmedicine.disease_causeMicrobiologyMolecular biologyMicrobiologyGene productEnterotoxinsPlasmidSubcloningGenes BacterialmedicineGenomic libraryCloning MolecularGeneEscherichia coliMicrobiology
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