Search results for "Erich"

showing 10 items of 805 documents

Norādījumi par tiesas resp. policijas obdukcijām

1925

Saturs: I. Vispārējie noteikumi 9 II. Līķa Izmeklēšanas kārtība 12 A) Ārējais apskats 13 B) Iekšējais apskats 17 a) Galvas dobuma izmeklēšana . 18 b) Ģīmja, zemaussdziedzeŗa (gl. parotis), dzirdes orgāna, aizdegunes (cavum nasopharyngeale) un acu izmeklēšana 22 c) Mugurkaulāja kanāla un muguras smadzeņu izmeklēšana. 22 d) Kakla, krūts un vēdera dobuma vispārējā izmeklēšana . 24 1) Krūts dobuma speciālā izmeklēšana 26 2) Kakla speciālā izmeklēšana. 29 3) Vēdera dobuma speciālā izmeklēšana 31 C) Līķu tiesmedicīniskā izmeklēšana saindēšanās gadījumos 35 D) Jaunpiedzimušo līķu tiesmedicīniskā izmeklēšana 39 E) Pārējie izmeklējumi 41 III. Līķa izmeklēšanas protokola un slēdziena sastādīšana 42 I…

GerichtsmedizinTiesu medicīna:MEDICINE::Morphology cell biology pathology::Pathology::Forensic medicine [Research Subject Categories]AutopsijaLīķu tiesmedicīniskā izmeklēšana
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Effect of Pseudomonas sp. MT5 baths on Flavobacterium columnare infection of rainbow trout and on microbial diversity on fish skin and gills

2005

Use of Pseudomonas sp. strain MT5 to prevent and treat Flavobacterium columnare infection was studied in 2 experiments with fingerling rainbow trout Oncorhynchus mykiss. In the first experiment, length heterogeneity analysis of PCR-amplified DNA fragments (LH-PCR) was used to assess the effect of antagonistic baths on the microbial diversity of healthy and experimentally infected fish. In the 148 samples studied, no difference was found between bathed and unbathed fish, and 3 fragment lengths were detected most frequently: 500 (in 75.7% of the samples), 523 (62.2%) and 517 bp (40.5%). The species contributing to these fragment sizes were Pseudomonas sp., Rhodococcus sp. and F. columnare, re…

GillsFish mortalityGillMolecular Sequence DataAquacultureAquatic ScienceFlavobacteriumPolymerase Chain ReactionColumnarisMicrobiologyFish DiseasesFlavobacteriaceae InfectionsPseudomonasImmersionEscherichia colimedicineAnimalsCloning MolecularEcology Evolution Behavior and SystematicsDNA PrimersSkinBase SequencebiologyPseudomonasSequence Analysis DNAbiology.organism_classificationmedicine.diseaseFlavobacteriaceaeElectroporationOncorhynchus mykissFlavobacterium columnareRainbow troutPseudomonadaceaeDiseases of Aquatic Organisms
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Giustizia sociale e libertà individuale. Antonio Rosmini e Friederich August von Hayek

2015

In questo saggio intendo far dialogare due dei maggiori rappresentanti della tradizione del liberalismo moderno e contemporaneo sul nesso giustizia/libertà. Il primo, Antonio Rosmini è l'esempio paradigmatico di pensatore religioso interessato a ‘pensare’ la storia con un approccio realista poco avvezzo alle utopie; il secondo, Friedrich August von Hayek, è uno dei membri più autorevoli diquella famosa Scuola Austriaca che a partire dal periodo fra le due guerre mondiali ha ingaggiato una lotta senza quartiere con la scuola keynesiana e con il socialismo sul modo in cui le istituzioni politiche devono interagire con il sistema di mercato.

Giustizia sociale libertà individuale Antonio Rosmini Friederich August von Hayek
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The inhibition of glycerol permeation through aquaglyceroporin-3 induced by mercury(II)

2016

Mercurial compounds are known to inhibit water permeation through aquaporins (AQPs). Although in the last years some hypotheses were proposed, the exact mechanism of inhibition is still an open question and even less is known about the inhibition of the glycerol permeation through aquaglyceroporins. Molecular dynamics (MD) simulations of human aquaporin-3 (AQP3) have been performed up to 200 ns in the presence of Hg2+ ions. For the first time, we have observed the unbiased passage of a glycerol molecule from the extracellular to cytosolic side. Moreover, the presence of Hg2+ ions covalently bound to Cys40 leads to a collapse of the aromatic/arginine selectivity filter (ar/R SF), blocking th…

Glycerol0301 basic medicineMolecular dynamicCell Membrane PermeabilityBiochemistryProtein Structure Secondarychemistry.chemical_compoundGLPFCOORDINATIONCRYSTALEscherichia coli ProteinsPermeationBiochemistryCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaPhosphatidylcholinesCOMPLEXESProtein BindingSTRUCTURAL BASISCations DivalentPlasmodium falciparumAquaporinCYSTEINE-189Molecular Dynamics SimulationMolecular dynamicsAquaporinsWATER CHANNELInorganic Chemistry03 medical and health sciencesEscherichia coliGlycerolExtracellularHumansMoleculePERMEABILITYProtein Structure QuaternaryAquaporin 3Binding SitesAQUAPORIN INHIBITIONWaterBiological TransportMembranes ArtificialAquaglyceroporinMercurySIMULATIONSProtein Structure TertiaryCytosolWater permeation030104 developmental biologyAquaglyceroporinschemistryStructural Homology ProteinBiophysicsGlycerol permeationJournal of Inorganic Biochemistry
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DcuA of aerobically grownEscherichia coliserves as a nitrogen shuttle (L‐aspartate/fumarate) for nitrogen uptake

2018

DcuA of Escherichia coli is known as an alternative C4 -dicarboxylate transporter for the main anaerobic C4 -dicarboxylate transporter DcuB. Since dcuA is expressed constitutively under aerobic and anaerobic conditions, DcuA was suggested to serve aerobically as a backup for the aerobic (DctA) transporter, or for the anabolic uptake of C4 -dicarboxylates. In this work, it is shown that DcuA is required for aerobic growth with L-aspartate as a nitrogen source, whereas for growth with L-aspartate as a carbon source, DctA was needed. Strains with DcuA catalyzed L-aspartate and C4 -dicarboxylate uptake (like DctA), or an L-aspartate/C4 -dicarboxylate antiport (unlike DctA). DcuA preferred L-asp…

Glycerol0301 basic medicineendocrine system diseasesAntiporter030106 microbiologyMalateschemistry.chemical_elementBiologymedicine.disease_causeMicrobiology03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsFumaratesAspartic acidEscherichia colimedicineGlycerolMolecular BiologyEscherichia coliDicarboxylic Acid TransportersAspartic AcidEscherichia coli Proteinsnutritional and metabolic diseasesBiological TransportTransporterbiology.organism_classificationNitrogen030104 developmental biologychemistryBiochemistryAnaerobic exercisehormones hormone substitutes and hormone antagonistsBacteriaMolecular Microbiology
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Functional citric acid cycle in an arcA mutant of Escherichia coli during growth with nitrate under anoxic conditions

1998

The operation of the citric acid cycle of Escherichia coli during nitrate respiration (anoxic conditions) was studied by measuring end products and enzyme activities. Excretion of products other than CO2, such as acetate or ethanol, was taken as an indication for a non-functional cycle. From glycerol, approximately 0.3 mol acetate was produced; the residual portion was completely oxidized, indicating the presence of a partially active citric acid cycle. In an arcA mutant devoid of the transcriptional regulator ArcA, glycerol was completely oxidized with nitrate as an electron acceptor, demonstrating derepression and function of the complete pathway. Glucose, on the other hand, was excreted …

GlycerolCitric Acid CycleDehydrogenasePseudomonas fluorescensPseudomonas fluorescensBiochemistryMicrobiologychemistry.chemical_compoundPseudomonasGenes RegulatorEscherichia coliGeneticsGlycerolAnaerobiosisMolecular BiologyDerepressionNitratesbiologySuccinate dehydrogenaseGeneral MedicineMetabolismbiology.organism_classificationPseudomonas stutzeriCitric acid cycleGlucoseBiochemistrychemistryGenes BacterialMutationbiology.proteinOxidation-ReductionArchives of Microbiology
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Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy

2021

High-resolution structural information on membrane proteins is essential for understanding cell biology and for the structure-based design of new medical drugs and drug delivery strategies. X-ray diffraction (XRD) can provide angstrom-level information about the structure of membrane proteins, yet for XRD experiments, proteins are removed from their native membrane environment, chemically stabilized, and crystallized, all of which can compromise the conformation. Here, we describe how a combination of surface-sensitive vibrational spectroscopy and molecular dynamics simulations can account for the native membrane environment. We observe the structure of a glycerol facilitator channel (GlpF)…

GlycerolInfrared spectroscopyAquaporinPROTEINAquaporinsVIBRATIONAL SPECTROSCOPYMolecular dynamicsCHANNELElectrochemistryGeneral Materials SciencePEPTIDESpectroscopyCRYSTALChemistryEscherichia coli ProteinsSpectrum AnalysisMembrane structureWaterSurfaces and InterfacesCondensed Matter PhysicsBILAYERGLYCEROLINTERFACEMembraneMembrane proteinMOLECULAR-DYNAMICSBiophysicsMembrane channelORIENTATIONSum frequency generation spectroscopy
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The GlpF residue Trp219 is part of an amino-acid cluster crucial for aquaglyceroporin oligomerization and function

2018

The vestibule loop regions of aquaglyceroporins are involved in accumulation of glycerol inside the channel pore. Even though most loop regions do not show high sequence similarity among aquaglyceroporins, loop E is highly conserved in aquaglyceroporins, but not in members of the homologous aquaporins. Specifically, a tryptophan residue is extremely conserved within this loop. We have investigated the role of this residue (Trp219) that deeply protrudes into the protein and potentially interacts with adjacent loops, using the E. coli aqualgyeroporin GlpF as a model. Replacement of Trp219 affects the activity of GlpF and impairs the stability of the tetrameric protein. Furthermore, we have id…

GlycerolModels Molecular0301 basic medicineProtein ConformationTetrameric proteinBiophysicsAquaporinAquaporinsBiochemistry03 medical and health sciencesResidue (chemistry)TetramerEscherichia coliAmino Acidschemistry.chemical_classification030102 biochemistry & molecular biologyProtein StabilityChemistryEscherichia coli ProteinsTryptophanTryptophanCell BiologyAmino acid030104 developmental biologyAquaglyceroporinsBiochemistryMutationBiophysicsProtein foldingProtein MultimerizationAquaglyceroporinsBiochimica et Biophysica Acta (BBA) - Biomembranes
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Microbial and chemical origins of the bactericidal activity of thermally treated yellow mustard powder toward Escherichia coli O157:H7 during dry sau…

2010

Abstract Work examines the origin of bactericidal activity in mustard flour and explores the relative contribution from starter cultures, E. coli O157:H7 itself and other sources. Bacteria can degrade naturally occurring glucosinolates in mustard and form isothiocyanates with antimicrobial activity. In the present work, 24 starter cultures (mostly from commercial mixtures) were screened for their capacity to decompose the glucosinolate, sinalbin. The most active pair, Pediococcus pentosaceus UM 121P and Staphylococcus carnosus UM 123M, were used together for the production of dry fermented sausage contaminated with E. coli O157:H7 (~ 6.5 log CFU/g). They were compared to industrial starters…

Glycoside HydrolasesStaphylococcusColony Count MicrobialFood ContaminationEscherichia coli O157medicine.disease_causeMicrobiologyCholineMicrobiologychemistry.chemical_compoundStarterIsothiocyanatesmedicinePediococcusFood scienceEscherichia coliStaphylococcus carnosusbiologyMyrosinasefood and beveragesGeneral MedicineAntimicrobialbiology.organism_classificationAnti-Bacterial AgentsSinalbinMeat ProductschemistryGlucosinolateFermentationFood MicrobiologyFermentationPowdersMustard PlantFood ScienceInternational Journal of Food Microbiology
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Probing suggested catalytic domains of glycosyltransferases by site-directed mutagenesis.

2003

The plant enzyme arbutin synthase isolated from cell suspension cultures of Rauvolfia serpentina and heterologously expressed in Escherichia coli is a member of the NRD1beta family of glycosyltransferases. This enzyme was used to prove, by site-directed mutagenesis, suggested catalytic domains and reaction mechanisms proposed for enzyme-catalyzed glycosylation. Replacement of amino acids far from the NRD domain do not significantly affect arbutin synthase activity. Exchange of amino acids at the NRD site leads to a decrease of enzymatic activity, e.g. substitution of Glu368 by Asp. Glu368, which is a conserved amino acid in glycosyltransferases located at position 2 and is important for enz…

GlycosylationStereochemistryMolecular Sequence DataBiologyBiochemistryPolymerase Chain ReactionGene Expression Regulation EnzymologicRauwolfiaSubstrate Specificitychemistry.chemical_compoundCatalytic DomainGlycosyltransferaseEscherichia coliAmino Acid SequenceSite-directed mutagenesisConserved SequenceDNA Primerschemistry.chemical_classificationBinding SitesATP synthaseSequence Homology Amino AcidMutagenesisArbutinGlycosyltransferasesEnzyme assayRecombinant ProteinsAmino acidEnzymechemistryBiochemistryAmino Acid Substitutionbiology.proteinMutagenesis Site-DirectedEuropean journal of biochemistry
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