Search results for "Erich"

showing 10 items of 805 documents

The effect of probiotics on the genotoxicity of furazolidone.

2004

Antigenotoxic activity of probiotic bacteria against furazolidone was studied using the short-term bacterial assay SOS chromotest, with Escherichia coli PQ37 as the test organism. The supernatants from probiotic and furazolidone co-incubation exhibited rather strong suppression on SOS induction produced by furazolidone on E. coli PQ 37 (sfiA: lacZ). Genotoxicity inhibition was found for all strains of the examined bacteria belonging to three genera. The highest genotoxicity inhibition was detected for Bifidobacterium lactis Bb-12 (92.0%) and for Lactobacillus acidophilus T20 (81.9%).

FurazolidoneBifidobacterium lactismedicine.disease_causeMicrobiologyMicrobiologylaw.inventionProbioticLactobacillus acidophiluslawmedicineSOS Response GeneticsEscherichia colibiologyMutagenicity TestsProbioticsFurazolidoneGeneral Medicinebiology.organism_classificationSOS chromotestLactobacillusAnti-Infective Agents LocalbacteriaBifidobacteriumBacteriaGenotoxicityFood Sciencemedicine.drugInternational journal of food microbiology
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Antibacterial activity of the enniatin B, produced by Fusarium tricinctum in liquid culture, and cytotoxic effects on Caco-2 cells.

2011

The enniatins (ENs) are bioactive compounds of hexadepsipeptidic structure produced by several strains of Fusarium sp. The EN B was purified from extracts of Fusarium tricinctum growth on liquid culture of potato dextrose broth (PDB), using a semipreparative liquid chromatography (LC) followed by an analytical LC. The purity and the structure of the isolated compound were confirmed by the determination of the extinction coefficient and with electrospray ionization-mass spectrometry (ESI-MS) study. The pure fraction of EN B was utilized to determine the antibiotic effects on several bacterial strains that are considered normally pathogens of the intestinal tract: Escherichia coli, Enterococc…

FusariumSpectrometry Mass Electrospray IonizationShigella dysenteriaeCell SurvivalHealth Toxicology and MutagenesisCell Culture TechniquesMicrobial Sensitivity TestsToxicologymedicine.disease_causeMicrobiologyListeria monocytogenesFusariumDepsipeptidesmedicineHumansYersinia enterocoliticaEscherichia colibiologyDose-Response Relationship DrugCell DifferentiationClostridium perfringensbiology.organism_classificationLipidsAnti-Bacterial AgentsCulture MediaSalmonella entericaCaco-2 CellsEnterococcus faeciumToxicology mechanisms and methods
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Isolation, purification and antibacterial effects of fusaproliferin produced by Fusariumsubglutinans in submerged culture.

2009

To evaluate the fusaproliferin (FUS) production, Fusariumsubglutinans ITEM 2404 was grown in a liquid medium of potato being this mycotoxin purified by high-performance liquid chromatography (HPLC) with a C18 semipreparative column using a mobile phase of acetonitrile/H(2)O using gradient conditions. The purity of the fusaproliferin was verified by analytical HPLC, ultraviolet absorbance measurements, LC/MS-MS, (1)H NMR spectroscopy. The isolated FUS was shown to be free of impurities and can be used as a standard for routine analysis. The pure fusaproliferin was utilized to study the biological activity on Escherichiacoli and Staphylococcusaureus. This study demostred that FUS not showed s…

FusariumSpectrometry Mass Electrospray IonizationStaphylococcus aureusChromatographyMagnetic Resonance SpectroscopybiologyChemistryTerpenesGeneral MedicineNuclear magnetic resonance spectroscopyToxicologybiology.organism_classificationAntimicrobialHigh-performance liquid chromatographyAnti-Bacterial AgentsFusarium subglutinanschemistry.chemical_compoundFusariumProton NMREscherichia coliMycotoxinChromatography High Pressure LiquidFood ScienceAntibacterial agentFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
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Escherichia coli cytolethal distending toxin blocks the HeLa cell cycle at the G2/M transition by preventing cdc2 protein kinase dephosphorylation an…

1997

Cytolethal distending toxins (CDT) constitute an emerging heterogeneous family of bacterial toxins whose common biological property is to inhibit the proliferation of cells in culture by blocking their cycle at G2/M phase. In this study, we investigated the molecular mechanisms underlying the block caused by CDT from Escherichia coli on synchronized HeLa cell cultures. To this end, we studied specifically the behavior of the two subunits of the complex that determines entry into mitosis, i.e., cyclin B1, the regulatory unit, and cdc2 protein kinase, the catalytic unit. We thus demonstrate that CDT causes cell accumulation in G2 and not in M, that it does not slow the progression of cells th…

G2 PhaseCytolethal distending toxinBacterial toxins[SDV]Life Sciences [q-bio]ImmunologyBacterial ToxinsMitosisBiologyMicrobiologyCDTCDC2 Protein KinaseEscherichia coliHumansKinase activityPhosphorylationMitosisCyclin-dependent kinase 1Cell growthCell CycleCell cycleG2-M DNA damage checkpointFlow CytometryMicrobiologie et ParasitologieCell biology[SDV] Life Sciences [q-bio]Enzyme ActivationInfectious DiseasesCytolethal distending toxinsParasitologyCDC2 Protein KinaseHeLa CellsResearch Article
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The Cell Cycle-Specific Growth-Inhibitory Factor Produced by Actinobacillus actinomycetemcomitans Is a Cytolethal Distending Toxin

1998

ABSTRACT Actinobacillus actinomycetemcomitans has been shown to produce a soluble cytotoxic factor(s) distinct from leukotoxin. We have identified in A. actinomycetemcomitans Y4 a cluster of genes encoding a cytolethal distending toxin (CDT). This new member of the CDT family is similar to the CDT produced by Haemophilus ducreyi . The CDT from A. actinomycetemcomitans was produced in Escherichia coli and was able to induce cell distension, growth arrest in G 2 /M phase, nucleus swelling, and chromatin fragmentation in HeLa cells. The three proteins, CDTA, -B and -C, encoded by the cdt locus were all required for toxin activity. Antiserum raised against recombinant CDTC completely inhibited …

G2 PhaseCytolethal distending toxin[SDV]Life Sciences [q-bio]Bacterial ToxinsMolecular Sequence DataRestriction MappingImmunologyMitosismedicine.disease_causeAggregatibacter actinomycetemcomitansMicrobiologyVirulence factorMicrobiologyEscherichia colimedicineHumansAmino Acid SequenceCloning MolecularEscherichia coliBase SequencebiologyToxinACTIVITEAggregatibacter actinomycetemcomitansGENETIQUECell cyclebiology.organism_classificationGrowth InhibitorsRecombinant Proteins[SDV] Life Sciences [q-bio]Infectious DiseasesGenes BacterialMultigene FamilyActinobacillusMolecular and Cellular PathogenesisParasitologyHaemophilus ducreyiHeLa CellsInfection and Immunity
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Type III Secretion-Dependent Cell Cycle Block Caused in HeLa Cells by Enteropathogenic Escherichia coliO103

2001

ABSTRACT Rabbit enteropathogenic Escherichia coli (EPEC) O103 induces in HeLa cells an irreversible cytopathic effect characterized by the recruitment of focal adhesions, formation of stress fibers, and inhibition of cell proliferation. We have characterized the modalities of the proliferation arrest and investigated its underlying mechanisms. We found that HeLa cells that were exposed to the rabbit EPEC O103 strain E22 progressively accumulated at 4C DNA content and did not enter mitosis. A significant proportion of the cells were able to reinitiate DNA synthesis without division, leading to 8C DNA content. This cell cycle inhibition by E22 was abrogated in mutants lacking EspA, -B, and -D…

G2 Phase[SDV]Life Sciences [q-bio]ImmunologyCyclin BMitosisReceptors Cell SurfacePATHOGENICITECyclin BMicrobiology03 medical and health sciencesBacterial ProteinsCDC2 Protein KinaseEscherichia coliHumansCyclin B1PhosphorylationCyclin B1Adhesins BacterialMitosisCytoskeleton030304 developmental biologyIntimin0303 health sciencesCyclin-dependent kinase 1Cellular Microbiology: Pathogen-Host Cell Molecular Interactionsbiology030306 microbiologyCell growthEscherichia coli ProteinsCell CycleREARRANGEMENTCell cycle[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyCell biology[SDV] Life Sciences [q-bio]Infectious Diseasesbiology.proteinTyrosineParasitologyCarrier ProteinsCDC2 Protein KinaseBacterial Outer Membrane ProteinsHeLa Cells
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Binding and/or hydrolysis of purine‐based nucleotides is not required for IM30 ring formation

2021

IM30, the inner membrane-associated protein of 30 kDa, is conserved in cyanobacteria and chloroplasts. Although its exact physiological function is still mysterious, IM30 is clearly essential for thylakoid membrane biogenesis and/or dynamics. Recently, a cryptic IM30 GTPase activity has been reported, albeit thus far no physiological function has been attributed to this. Yet, it is still possible that GTP binding/hydrolysis affects formation of the prototypical large homo-oligomeric IM30 ring and rod structures. Here, we show that the Synechocystis sp. PCC 6803 IM30 protein in fact is an NTPase that hydrolyzes GTP and ATP, but not CTP or UTP, with about identical rates. While IM30 forms lar…

GTP'Genetic VectorsBiophysicsGene ExpressionGTPaseRing (chemistry)ThylakoidsBiochemistrySubstrate Specificity03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsStructural BiologyEscherichia coliGeneticsNucleotideddc:610Cloning MolecularMolecular BiologyEnzyme Assays030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryHydrolysis030302 biochemistry & molecular biologySynechocystisSynechocystisMembrane ProteinsCell BiologyNucleoside-Triphosphatasebiology.organism_classificationRecombinant ProteinsKineticsMicroscopy ElectronThylakoidMembrane biogenesisBiophysicsGuanosine TriphosphateBiogenesisProtein BindingFEBS Letters
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The tetrameric α-helical membrane protein GlpF unfolds via a dimeric folding intermediate.

2011

Many membrane proteins appear to be present and functional in higher-order oligomeric states. While few studies have analyzed the thermodynamic stability of α-helical transmembrane (TM) proteins under equilibrium conditions in the past, oligomerization of larger polytopic monomers has essentially not yet been studied. However, it is vital to study the folding of oligomeric membrane proteins to improve our understanding of the general mechanisms and pathways of TM protein folding. To investigate the folding and stability of the aquaglyceroporin GlpF from Escherichia coli, unfolding of the protein in mixed micelles was monitored by steady-state fluorescence and circular dichroism spectroscopy…

Gel electrophoresisCircular dichroismProtein FoldingChemistryCircular DichroismEscherichia coli ProteinsMembrane ProteinsAquaporinsBiochemistryMicelleTransmembrane proteinProtein Structure SecondaryFolding (chemistry)CrystallographyKineticsMembrane proteinBiophysicsEscherichia coliProtein foldingChemical stabilityDimerizationProtein UnfoldingBiochemistry
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MboII endonuclease heat inactivation before agarose gel electrophoresis to prevent artifactual bands in restriction patterns

1999

Gel electrophoresisDNA BacterialElectrophoresis Agar GelProtein DenaturationSettore MED/07 - Microbiologia E Microbiologia ClinicaHot TemperaturebiologyMolecular biologyGeneral Biochemistry Genetics and Molecular BiologyRestriction fragmentHeat inactivationElectrophoresischemistry.chemical_compoundRestriction enzymeBiochemistrychemistryAgarose gel electrophoresisEnzyme Stabilitybiology.proteinEscherichia coliDeoxyribonucleases Type II Site-SpecificMboII endonucleaseDNAPolymorphism Restriction Fragment LengthBiotechnology
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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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