Search results for "Erich"

showing 10 items of 805 documents

Evaluation of dermal toxicity of antibacterial cotton textile coated by sol-gel technology

2017

AbstractThis paper reports about cotton textile modification by sol-gel technology with the purpose of obtaining antibacterial properties, evaluation of antibacterial properties and dermal toxicity tests of cotton textile with Zn and Si coating. Antibacterial properties evaluation against pathogenic microorganisms Pseudomonas aeruginosa, Staphylococcus aureus, and Escherichia coli made using the Parallel streak method in accordance with ATCC147 standard. For more specific evaluation of the coated textile, in vitro cytotoxicity test with epidermal HaCat cells was done. It is concluded that the coatings containing Zn and Si obtained by the sol-gel technology can impart antibacterial propertie…

TextilePolymers and PlasticsMaterials Science (miscellaneous)Microorganism02 engineering and technologyengineering.materialmedicine.disease_cause01 natural sciencesIndustrial and Manufacturing EngineeringCoating0103 physical sciencesmedicineFood scienceComposite materialEscherichia coli010302 applied physicsintegumentary systembiologyChemistrybusiness.industryPathogenic bacteria021001 nanoscience & nanotechnologybiology.organism_classificationHaCaTStaphylococcus aureusengineering0210 nano-technologyGeneral Agricultural and Biological SciencesbusinessBacteriaThe Journal of The Textile Institute
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Combining in the melt physical and biological properties of poly(caprolactone) and chlorhexidine to obtain antimicrobial surgical monofilaments.

2012

Bacterial infections on a sutured wound represent a critical problem, and the preparation of suture threads possessing antimicrobial properties is valuable. In this work, poly(caprolactone) (PCL) monofilaments were compounded at the concentration of 1, 2 and 4 % (w/w), respectively, to the antiseptic chlorhexidine diacetate (CHX). The incorporation was carried out in the melt by a single-step methodology, i.e. “online” approach. Mechanical tests revealed that the incorporation of CHX does not significantly change tensile properties of PCL fibres as the thermal profile adopted to prepare the compounded fibres does not compromise the antibacterial activity of CHX. In fact, CHX confers to comp…

Thermoplasticmedicine.drug_classCell SurvivalPolyestersSettore BIO/19 - Microbiologia GeneraleApplied Microbiology and Biotechnologychemistry.chemical_compoundAntisepticTensile StrengthPolymer chemistryUltimate tensile strengthmedicineEscherichia coliHumanschemistry.chemical_classificationpoly(caprolactone)biologyChemistryChlorhexidinechlorhexidineChlorhexidineSuture TechniquesSpectrometry X-Ray EmissionGeneral MedicineFibroblastsbiology.organism_classificationAntimicrobialMicrococcus luteusSettore ING-IND/22 - Scienza E Tecnologia Dei MaterialiEquipment and Suppliessurgical monofilamentsAnti-Infective Agents LocalMicroscopy Electron ScanningMicrococcus luteusAntibacterial activityCaprolactoneBiotechnologyNuclear chemistrymedicine.drugBacillus subtilisApplied microbiology and biotechnology
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Thiosulfate Reduction in Salmonella enterica Is Driven by the Proton Motive Force

2012

ABSTRACT Thiosulfate respiration in Salmonella enterica serovar Typhimurium is catalyzed by the membrane-bound enzyme thiosulfate reductase. Experiments with quinone biosynthesis mutants show that menaquinol is the sole electron donor to thiosulfate reductase. However, the reduction of thiosulfate by menaquinol is highly endergonic under standard conditions (Δ E °′ = −328 mV). Thiosulfate reductase activity was found to depend on the proton motive force (PMF) across the cytoplasmic membrane. A structural model for thiosulfate reductase suggests that the PMF drives endergonic electron flow within the enzyme by a reverse loop mechanism. Thiosulfate reductase was able to catalyze the combined …

ThiosulfatesSulfurtransferaseElectron donorNaphtholsBiologyPhotochemistryMicrobiologyGene Expression Regulation Enzymologicchemistry.chemical_compoundElectron transferSulfiteEscherichia coliFormateMolecular BiologyExergonic reactionThiosulfateTerpenesChemiosmosisProton-Motive ForceSalmonella entericaGene Expression Regulation BacterialArticleschemistryBiochemistrySulfurtransferasesThermodynamicsProtonsOxidation-ReductionJournal of Bacteriology
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Fluorescence Properties of the Chromophore-Binding Domain of Bacteriophytochrome from Deinococcus radiodurans

2013

Fluorescent proteins are versatile tools for molecular imaging. In this study, we report a detailed analysis of the absorption and fluorescence properties of the chromophore-binding domain from Deinococcus radiodurans and its D207H mutant. Using single photon counting and transient absorption techniques, the average excited state lifetime of both studied systems was about 370 ps. The D207H mutation slightly changed the excited state decay profile but did not have a considerable effect on the average decay time of the system or the shape of the absorption and emission spectra of the biliverdin chromophore. We confirmed that the fluorescence properties of both samples are very similar in vivo…

Time FactorsFluorescence in the life sciencesPhotochemistrychemistry.chemical_compoundBimolecular fluorescence complementationBacterial ProteinsEscherichia coliMaterials ChemistryPhysical and Theoretical Chemistryta116BiliverdinbiologyPhytochromeBiliverdineta1182Deinococcus radioduransChromophorebiology.organism_classificationFluorescenceRecombinant ProteinsProtein Structure TertiarySurfaces Coatings and FilmschemistryMutationQuantum TheorySpectrophotometry UltravioletDeinococcusBinding domainThe Journal of Physical Chemistry B
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Function of DcuS from Escherichia coli as a Fumarate-stimulated Histidine Protein Kinase in Vitro

2002

The two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C(4)-dicarboxylate metabolism in response to extracellular C(4)- dicarboxylates such as fumarate or succinate. DcuS is a membrane-integral sensor kinase, and the sensory and kinase domains are located on opposite sides of the cytoplasmic membrane. The intact DcuS protein (His(6)-DcuS) was overproduced and isolated in detergent containing buffer. His(6)-DcuS was reconstituted into liposomes made from E. coli phospholipids. Reconstituted His(6)-DcuS catalyzed, in contrast to the detergent-solubilized sensor, autophosphorylation by [gamma-(33)P]ATP with an approximate K(D) of 0.16 mm for ATP. Up t…

Time FactorsHistidine KinaseProteolipidsDetergentsBiologymedicine.disease_causeModels BiologicalBiochemistryAdenosine TriphosphateFumaratesEscherichia colimedicinePhosphorylationPromoter Regions GeneticProtein kinase AMolecular BiologyEscherichia coliDose-Response Relationship DrugKinaseEscherichia coli ProteinsCell MembraneAutophosphorylationDNACell BiologyTransmembrane proteinDNA-Binding ProteinsKineticsResponse regulatorBiochemistryLiposomesPhosphorylationSignal transductionProtein KinasesProtein BindingSignal TransductionTranscription FactorsJournal of Biological Chemistry
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Robust dynamical pattern formation from a multifunctional minimal genetic circuit.

2010

Abstract Background A practical problem during the analysis of natural networks is their complexity, thus the use of synthetic circuits would allow to unveil the natural mechanisms of operation. Autocatalytic gene regulatory networks play an important role in shaping the development of multicellular organisms, whereas oscillatory circuits are used to control gene expression under variable environments such as the light-dark cycle. Results We propose a new mechanism to generate developmental patterns and oscillations using a minimal number of genes. For this, we design a synthetic gene circuit with an antagonistic self-regulation to study the spatio-temporal control of protein expression. He…

Time FactorsTranscription GeneticSystems biologyGene regulatory networkPattern formationBiologyModels BiologicalCatalysis03 medical and health sciences0302 clinical medicineStructural BiologyModelling and SimulationOscillometryResearch articleEscherichia coliGene Regulatory Networkslcsh:QH301-705.5Molecular Biology030304 developmental biologyElectronic circuitGeneticsRegulation of gene expression0303 health sciencesModels StatisticalModels GeneticMechanism (biology)Applied MathematicsQuantitative Biology::Molecular NetworksGene Expression ProfilingSystems BiologyRobustness (evolution)DNAComputer Science ApplicationsQuorum sensinglcsh:Biology (General)Gene Expression RegulationModeling and SimulationBiological system030217 neurology & neurosurgeryBMC systems biology
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Role of tir and intimin in the virulence of rabbit enteropathogenic Escherichia coli serotype O103:H2.

2000

ABSTRACT Attaching and effacing (A/E) rabbit enteropathogenic Escherichia coli (REPEC) strains belonging to serogroup O103 are an important cause of diarrhea in weaned rabbits. Like human EPEC strains, they possess the locus of enterocyte effacement clustering the genes involved in the formation of the A/E lesions. In addition, pathogenic REPEC O103 strains produce an Esp-dependent but Eae (intimin)-independent alteration of the host cell cytoskeleton characterized by the formation of focal adhesion complexes and the reorganization of the actin cytoskeleton into bundles of stress fibers. To investigate the role of intimin and its translocated coreceptor (Tir) in the pathogenicity of REPEC, …

Time Factors[SDV]Life Sciences [q-bio]MutantAdministration OralPATHOGENICITEmedicine.disease_causeBacterial AdhesionMICROSCOPIE ELECTRONIQUE A TRANSMISSIONFecesCytoskeleton0303 health sciencesVirulenceEscherichia coli ProteinsEnterobacteriaceae3. Good health[SDV] Life Sciences [q-bio]IntestinesInfectious DiseasesMolecular and Cellular PathogenesisRabbitsLocus of enterocyte effacementBacterial Outer Membrane ProteinsImmunologyMolecular Sequence DataVirulenceReceptors Cell SurfaceBiologyMicrobiologydigestive systemMicrobiologyCell Line03 medical and health sciencesBacterial ProteinsIleummedicineEscherichia coliAnimalsHumansEnteropathogenic Escherichia coliAdhesins BacterialEscherichia coli030304 developmental biologyIntiminModels Genetic030306 microbiologyGenetic Complementation TestEpithelial Cellsbiochemical phenomena metabolism and nutritionbiology.organism_classificationActin cytoskeleton[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyActinsKineticsMicroscopy ElectronMicroscopy FluorescenceMutagenesisParasitologyCarrier ProteinsHeLa CellsInfection and immunity
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Molecular characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum: gene cloning, transcriptional analysis, overex…

1997

By using degenerate primers designed from the first 19 N-terminal amino acids of Lactobacillus plantarum p-coumaric acid decarboxylase (PDC), a 56-bp fragment was amplified from L. plantarum in PCRs and used as a probe for screening an L. plantarum genomic bank. Of the 2,880 clones in the genomic bank, one was isolated by colony hybridization and contained a 519-bp open reading frame (pdc gene) followed by a putative terminator structure. The pdc gene is expressed on a monocistronic transcriptional unit, which is transcribed from promoter sequences homologous to Lactococcus promoter sequences. No mRNA from pdc and no PDC activity were detected in uninduced cell extracts, indicating that the…

Transcription GeneticCarboxy-LyasesMolecular Sequence Datamacromolecular substancesMolecular cloningmedicine.disease_causePolymerase Chain ReactionApplied Microbiology and BiotechnologyOpen Reading FramesLactococcusGene expressionEscherichia colimedicineGenomic libraryAmino Acid SequenceCloning MolecularPromoter Regions GeneticEscherichia coliGeneGene LibraryRecombination GeneticElectronic Data ProcessingBase SequenceEcologybiologyNucleic acid sequenceChromosome MappingNucleic Acid Hybridizationhemic and immune systemsGene Expression Regulation BacterialBlotting Northernbiology.organism_classificationMolecular biologyRecombinant ProteinsBlotting SouthernLactobacillusRNA BacterialTerminator (genetics)BiochemistryEnzyme InductionElectrophoresis Polyacrylamide GelLactobacillus plantarumResearch ArticleFood ScienceBiotechnologyApplied and Environmental Microbiology
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Transcriptional analysis of the nitrile‐degrading operon from Rhodococcus sp. ACV2 and high level production of recombinant amidase with an Escherich…

1999

Northern blotting analysis with RNA probes derived from amidase and nitrile hydratase genes from Rhodococcus sp. ACV2 revealed that both genes are part of the same operon. RNase protection mapping and sequence analysis indicated that the operon is probably under the control of a sigma 70-like promoter located upstream from the amidase gene. Plasmids were constructed with the cloned genes under tac and lac promoter control. Expression of amdA was demonstrated in Escherichia coli. In another construction, the amdA gene was inserted under the control of the bacteriophage T7 promoter. Large amounts of recombinant amidase (at least 20% of total proteins) in a soluble and active form were obtaine…

Transcription GeneticOperonMolecular Sequence Datalac operonBiologymedicine.disease_causeApplied Microbiology and BiotechnologyAmidohydrolasesAmidase03 medical and health sciencesPlasmidNitrile hydrataseBacteriophage T7OperonGene expressionEscherichia colimedicineAmidase activityRhodococcus[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyEscherichia coliHydro-LyasesComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesBase Sequence030306 microbiologyGeneral MedicineMolecular biologyRecombinant Proteins[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryGenes BacterialBiotechnologyJournal of Applied Microbiology
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The dnaK operon of Streptomyces coelicolor encodes a novel heat-shock protein which binds to the promoter region of the operon

1995

Transcriptional studies have demonstrated that the dnaK gene of Streptomyces coelicolor A3(2) is contained within a 4.3 kb operon. The operon is transcribed from a single (transiently) heat-inducible promoter, dnaKp, that resembles the typical vegetative (sigma 70-recognized) eubacterial consensus promoter sequence. dnaK transcription was found to be heat-inducible at all stages of development in surface-grown cultures. In addition, at the normal growth temperature of 30 degrees C, dnaK transcript levels were shown to vary at different stages of development, being more abundant in young germinating cultures and in mycelium undergoing sporogenesis. The nucleotide sequence of the dnaK operon …

Transcription GeneticOperonMolecular Sequence Datalac operonRepressorMicrobiologytrp operonOpen Reading FramesOperonEscherichia coligal operonHSP70 Heat-Shock ProteinsAmino Acid SequencePromoter Regions GeneticMolecular BiologyHeat-Shock ProteinsGeneticsBinding SitesBase SequenceSequence Homology Amino AcidbiologyEscherichia coli ProteinsStreptomyces coelicolorCell DifferentiationPromoterGene Expression Regulation BacterialBlotting Northernbiology.organism_classificationMolecular biologyRecombinant ProteinsStreptomycesGenes BacterialbacteriaL-arabinose operonHeat-Shock ResponseProtein BindingMolecular Microbiology
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