Search results for "Chickens"

showing 10 items of 147 documents

The role of choline in the release of acetylcholine in isolated hearts.

1978

1. The concentrations of acetylcholine, choline and noradrenaline were estimated in the perfusate (overflow) of isolated hearts of chickens, cats, rabbits and guinea pigs. Neurotransmitter release was evoked by stimulation of both vagus nerves and by direct stimulation of the heart (field stimulation). 2. In the absence of exogenous choline and physostigmine, field stimulation at 20 Hz for 20 min caused an overflow of acetylcholine from the hearts of the 4 species investigated. During vagal stimulation, however, acetylcholine was detected only in the perfusate of the chicken heart. 3. Field stimulation for 2 min caused an overflow of 193 pmol g−1 min−1 acetylcholine and of 666 pmol g−1 min−…

Malemedicine.medical_specialtyPhysostigmineanimal structuresReserpinePhysostigmineGuinea PigsStimulationIn Vitro TechniquesCholinechemistry.chemical_compoundNorepinephrineInternal medicinemedicineCholineAnimalsNeurotransmitterGanglia AutonomicCholinesterasePharmacologybiologyMyocardiumVagus NerveGeneral MedicineReserpineAcetylcholineElectric StimulationEndocrinologychemistrybiology.proteinCatsCholinergicFemaleRabbitsChickensAcetylcholinemedicine.drugNaunyn-Schmiedeberg's archives of pharmacology
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Evidence for noradrenaline and adrenaline as sympathetic transmitters in the chicken.

1975

1 The concentrations of noradrenaline and adrenaline in various organs, arterial plasma and venous outflow from isolated hearts of adult chickens have been determined. 2 The relative adrenaline concentrations (percentage of the sum of noradrenaline and adrenaline) in the heart (33%), spleen (16%) and brain (26%) were higher than those found in mammalian organs. Chemical sympathectomy by pretreatment with 6-hydroxydopamine caused a decrease of the noradrenaline and adrenaline concentrations in the heart to 20 and 23% and in the spleen to 16 and 29%, respectively. 3 Stimulation of the right sympathetic nerves, infusion of tyramine or infusion of a modified Tyrode solution containing 108mM K+ …

Malemedicine.medical_specialtySympathetic nervous systemSympathetic Nervous SystemEpinephrineAdrenergicTyramineStimulationBlood PressureIn Vitro TechniquesNorepinephrine (medication)chemistry.chemical_compoundHydroxydopaminesNorepinephrineCatecholaminesInternal medicinemedicineAnimalsPharmacologyNeurotransmitter AgentsHeartTyramineAtrial FunctionElectric StimulationCardiovascular physiologyEpinephrineEndocrinologymedicine.anatomical_structureBlood pressurechemistryPotassiumChickensmedicine.drugResearch ArticleBritish journal of pharmacology
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Cytochalasin B selectively releases ovalbumin mRNA precursors but not the mature ovalbumin mRNA from hen oviduct nuclear matrix

1987

Hen oviduct nuclear matrix-bound mature ovalbumin mRNA is released from the matrix in the presence of ATP, while the ovalbumin mRNA precursors remain bound to this structure. Detachment of the mature mRNA from the matrix by ATP as well as ATP-dependent efflux of mRNA from isolated nuclei were found to be inhibited by cytochalasin B. On the other hand, in the absence of ATP, cytochalasin B exclusively caused the release (and nucleocytoplasmic efflux) of the ovalbumin messenger precursors, but not of the mature mRNA. After cytochalasin B treatment, actin could be detected in the matrix supernatant. Phalloidin which stabilizes actin filaments did not cause RNA liberation in the absence of ATP,…

Mature messenger RNACytochalasin BOvalbuminPhalloidinePhalloidinOviductsmacromolecular substancesBiologyBiochemistrychemistry.chemical_compoundAdenosine TriphosphateRNA PrecursorsAnimalsCytochalasinRNA MessengerIntermediate filamentCytochalasin BCell NucleusMessenger RNAAntibodies MonoclonalNucleic Acid PrecursorsNuclear matrixMolecular biologyOvalbuminchemistrybiology.proteinFemaleChickensEuropean Journal of Biochemistry
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Presence of mycotoxins in ready-to-eat food and subsequent risk assessment

2018

Abstract A study on a set of ready-to-eat meals (n = 328) based on cereals, legumes, vegetables, fish and meat was carried out to determine the natural presence of twenty-seven mycotoxins by both liquid chromatography and gas chromatography coupled mass spectrometry in tandem (MS/MS) after QuEChERS extraction. The occurrence of mycotoxins was headed by cereal samples with 35% of samples contaminated by at least one mycotoxin followed by vegetables (32%), legumes (15%) and lastly, 9% of fish and meat samples were contaminated. DON was the most detected mycotoxin in vegetables, meat, fish and cereals with an incidence of 13% 18% 19% and 60%, respectively, and the highest mean levels were foun…

MeatFood HandlingSwineFood ContaminationBiologyToxicologyQuechersmedicine.disease_causeRisk Assessment01 natural sciencesFood groupchemistry.chemical_compound0404 agricultural biotechnologyVegetablesmedicineAnimalsFood scienceMycotoxinLegumeToxin010401 analytical chemistryFishesfood and beveragesFabaceae04 agricultural and veterinary sciencesGeneral MedicineMycotoxinsContamination040401 food science0104 chemical scienceschemistryReady to eat foodCattleGas chromatographyEdible GrainChickensFood ScienceFood and Chemical Toxicology
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Circadian gene expression patterns of melanopsin and pinopsin in the chick pineal gland

2004

The directly light-sensitive chick pineal gland contains at least two photopigments. Pinopsin seems to mediate the acute inhibitory effect of light on melatonin synthesis, whereas melanopsin may act by phase-shifting the intrapineal circadian clock. In the present study we have investigated, by means of quantitative RT-PCR, the daily rhythm of photopigment gene expression as monitored by mRNA levels. Under a 12-h light/12-h dark cycle, the mRNA levels of both pigments were 5-fold higher in the transitional phase from light to dark than at night, both in vivo and in vitro. Under constant darkness in vivo and in vitro, the peak of pinopsin mRNA levels was attenuated, whereas that of melanopsi…

Melanopsinmedicine.medical_specialtyLightPhotoperiodCircadian clockBiophysicsNerve Tissue ProteinsBiologyPineal GlandBiochemistryAvian ProteinsPineal glandInternal medicineGene expressionmedicineAnimalsPhotopigmentCircadian rhythmMolecular BiologyCells CulturedRegulation of gene expressionAdaptation OcularRod OpsinsCell BiologyCircadian Rhythmmedicine.anatomical_structureEndocrinologyAnimals NewbornGene Expression RegulationLight effects on circadian rhythmsense organsChickensBiochemical and Biophysical Research Communications
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VanB-VanC1 Enterococcus gallinarum, Italy

2005

To the Editor: We report detecting a vanB determinant in Enterococcus gallinarum in poultry in Italy. High-level vanA-mediated glycopeptide resistance has been described for E. gallinarum and E. casseliflavus (1–4), and vanB-mediated vancomycin resistance has been frequently described for E. faecalis and E. faecium. However, vanB-mediated resistance in isolates of E. gallinarum has been described only in sporadic nosocomial cases of infection or colonization (5,6). In January 2005, a study of contamination by foodborne organisms in slaughtered broiler carcasses was conducted in Sicily. To detect glycopeptide-resistant enterococci (GRE), each carcass was placed in a bag with 100 mL sterile b…

Microbiology (medical)Epidemiologyeducationletterlcsh:MedicineMicrobial Sensitivity TestsEnteococcus gallinarum; vanB-vanC1lcsh:Infectious and parasitic diseasesMicrobiologychemistry.chemical_compoundEnterococcus gallinarumBacterial ProteinsMultiplex polymerase chain reactionmedicineAnimalsmedia_common.cataloged_instancelcsh:RC109-216Peptide SynthasesEuropean unionLetters to the Editormedia_commonbiologyTeicoplaninpoultryEnterococcus gallinarumlcsh:RAvoparcinVancomycin Resistancebiochemical phenomena metabolism and nutritionvancomycin-resistant enterococcibacterial infections and mycosesbiology.organism_classificationGlycopeptideInfectious DiseasesEnterococcuschemistryItalyVancomycinvanB-vanC1ChickensEnterococcusmedicine.drug
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Design and construction of highly stable, protease-resistant chimeric avidins.

2005

The chicken avidin gene family consists of avidin and seven separate avidin-related genes (AVRs) 1-7. Avidin protein is a widely used biochemical tool, whereas the other family members have only recently been produced as recombinant proteins and characterized. In our previous study, AVR4 was found to be the most stable biotin binding protein thus far characterized (T(m) = 106.4 degrees C). In this study, we studied further the biotin-binding properties of AVR4. A decrease in the energy barrier between the biotin-bound and unbound state of AVR4 was observed when compared with that of avidin. The high resolution structure of AVR4 facilitated comparison of the structural details of avidin and …

Models MolecularBiotin bindingInsectaProtein familyProtein subunitRecombinant Fusion ProteinsMolecular Sequence DataBiotinBiosensing TechniquesBiologyProtein EngineeringBiochemistryProtein Structure SecondaryProtein structureAnimalsAmino Acid SequenceMolecular BiologyThermostabilityCalorimetry Differential ScanningSequence Homology Amino AcidTemperatureCell BiologyProtein engineeringAvidinRecombinant ProteinsProtein Structure TertiaryKineticsBiochemistryMicroscopy FluorescenceMutagenesisBiotinylationMutationbiology.proteinChromatography GelThermodynamicsElectrophoresis Polyacrylamide GelEndopeptidase KBaculoviridaeChickensAvidinChromatography LiquidPeptide HydrolasesProtein BindingThe Journal of biological chemistry
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Construction of a dual chain pseudotetrameric chicken avidin by combining two circularly permuted avidins.

2004

Two distinct circularly permuted forms of chicken avidin were designed with the aim of constructing a fusion avidin containing two biotin-binding sites in one polypeptide. The old N and C termini of wild-type avidin were connected to each other via a glycine/serine-rich linker, and the new termini were introduced into two different loops. This enabled the creation of the desired fusion construct using a short linker peptide between the two different circularly permuted subunits. The circularly permuted avidins (circularly permuted avidin 5 → 4 and circularly permuted avidin 6 → 5) and their fusion, pseudotetrameric dual chain avidin, were biologically active, i.e. showed biotin binding, and…

Models MolecularBiotin bindingProtein DenaturationProtein FoldingStereochemistryProtein ConformationProtein subunitMolecular Sequence DataGlycineBiotinBiochemistrySensitivity and SpecificityProtein Structure Secondarystomatognathic systemChain (algebraic topology)SerineAnimalsAmino Acid SequenceBinding siteProtein Structure QuaternaryMolecular BiologyLinker peptideBinding SitesbiologyCell Biologyrespiratory systemAvidinProtein Structure TertiaryCrystallographyKineticsMutationbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelEndopeptidase KPeptidesLinkerChickensAvidinProtein BindingThe Journal of biological chemistry
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Tetravalent single-chain avidin: from subunits to protein domains via circularly permuted avidins

2005

scAvd (single-chain avidin, where two dcAvd are joined in a single polypeptide chain), having four biotin-binding domains, was constructed by fusion of topologically modified avidin units. scAvd showed similar biotin binding and thermal stability properties as chicken avidin. The DNA construct encoding scAvd contains four circularly permuted avidin domains, plus short linkers connecting the four domains into a single polypeptide chain. In contrast with wild-type avidin, which contains four identical avidin monomers, scAvd enables each one of the four avidin domains to be independently modified by protein engineering. Therefore the scAvd scaffold can be used to construct spatially and stoich…

Models MolecularBiotin bindingProtein domainMolecular Sequence DataProtein EngineeringBiochemistrychemistry.chemical_compoundMoleculeAnimalsMolecular BiologyCells CulturedBinding SitesbiologyChemistryCell BiologyProtein engineeringCircular permutation in proteinsAvidinProtein Structure TertiaryCrystallographyProtein SubunitsMonomerBiophysicsbiology.proteinDNA constructChickensAvidinResearch ArticleProtein Binding
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Conformational Changes in the Nucleosome Followed by the Selective Accessibility of Histone Glutamines in the Transglutaminase Reaction:  Effects of …

2001

Transglutaminases, the enzymes that catalyze the acyl-transfer reaction between glutamine and primary amines, have been used to introduce probes into proteins in order to perform structural studies using physical techniques. Here we use an original approach in which the increasing accessibility of the glutamines of core histones to TGase is used to monitor the salt-induced conformational changes of the nucleosome. The rationale of this strategy is that the accessibility of a glutamine to transglutaminase depends on the blockage due to the presence of either other histones or DNA. At low ionic strength, only glutamines on the N-terminal tails of H2B and H3 are labeled with monodansylcadaveri…

Models MolecularMacromolecular SubstancesProtein ConformationTissue transglutaminaseGlutamineBiochemistryCatalysisHistoneschemistry.chemical_compoundProtein structureTetramerCadaverineAnimalsNucleosomeComputer Simulationchemistry.chemical_classificationTransglutaminasesbiologyOsmolar ConcentrationDNANucleosomesHistoneEnzymechemistryBiochemistryIonic strengthbiology.proteinChickensDimerizationDNABiochemistry
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