Search results for "bovine"

showing 10 items of 271 documents

Détection culturale et moléculaire de Mycobacterium bovis, l'agent de la tuberculose bovine, dans les matrices environnementales

2013

[SDV] Life Sciences [q-bio][SDE] Environmental Sciences[SDV]Life Sciences [q-bio]tuberculose bovine[SDE]Environmental Sciencesdetection[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyMycobacterium bovis
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La tuberculose bovine en Côte-d’Or : Statut épidémiologique et rôle du blaireau (Meles meles)

2013

Rapport de Stage de Master 2 EA MERS CT3; Master

[SDV] Life Sciences [q-bio][SDE] Environmental SciencesblaireauxCôte d'Or[SDV]Life Sciences [q-bio]tuberculose bovine[SDE]Environmental Sciences[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyMeles meles
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Estimation de la densité du Blaireau (Meles meles) en Côte d’Or au regard du risque de transmission de la tuberculose bovine

2012

Rapport de Stage de Master 2 EA MERS CT3; Master

[SDV] Life Sciences [q-bio]blaireauxCôte d'Or[SDV]Life Sciences [q-bio]tuberculose bovinetaux de contactpopulationMeles meles
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Widespread diminishing anthropogenic effects on calcium in freshwaters

2019

Calcium (Ca) is an essential element for almost all living organisms. Here, we examined global variation and controls of freshwater Ca concentrations, using 440 599 water samples from 43 184 inland water sites in 57 countries. We found that the global median Ca concentration was 4.0 mg L−1 with 20.7% of the water samples showing Ca concentrations ≤ 1.5 mg L−1 , a threshold considered critical for the survival of many Ca-demanding organisms. Spatially, freshwater Ca concentrations were strongly and proportionally linked to carbonate alkalinity, with the highest Ca and carbonate alkalinity in waters with a pH around 8.0 and decreasing in concentrations towards lower pH. However, on a temporal…

[SDV]Life Sciences [q-bio][SDE.MCG]Environmental Sciences/Global Changesalkalinitylcsh:MedicineArticleIsolationanthropogenic effectsEnvironmental impactbiogeochemistryanthropiqueLake Geneva Abbreviations: BALO: Bdellovibrio and Like OrganismsSettore BIO/07 - ECOLOGIAElement cyclesfreshwatersBdellovibrio spfreshwaterlcsh:ScienceEkologicalciumEcologyBSA: Bovine Serum Albuminlcsh:Rtrendeau douce[SDU]Sciences of the Universe [physics]Bacterial PredatorSDS: Sodium Dodecyl Sulfate[SDE]Environmental SciencesarticlesFreshwater ecologylcsh:QPreysScientific Reports
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Utilizzo del pisello proteico in alternativa alla farina di estrazione di soia in un allevamento biologico di bovine da latte

2008

Utilizzazione del pisello proteico in alternativa alla farina di estrazione di soia in un allevamento biologico di bovine da latte. Nella sperimentazione è stata verificata la possibilità di impiego del pisello proteico in sostituzione totale della farina di estrazione di soia nel concentrato destinato a bovine da latte allevate in regime biologico. Sono state utilizzate 14 bovine di razza Bruna suddivise in due gruppi omogenei ognuno alimentato, per l’intera durata della prova (292 d), con uno dei due diversi concentrati. La produzione di latte non si è differenziata fra i gruppi, sebbene le bovine che ricevevano il pisello proteico abbiano prodotto, rispetto alla soia, una quantità di lat…

allevamento biologico bovine latte pisello proteico
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Potential anticarcinogenic peptides from bovine milk.

2012

Bovine milk possesses a protein system constituted by two major families of proteins: caseins (insoluble) and whey proteins (soluble). Caseins (αS1,αS2,β, andκ) are the predominant phosphoproteins in the milk of ruminants, accounting for about 80% of total protein, while the whey proteins, representing approximately 20% of milk protein fraction, includeβ-lactoglobulin,α-lactalbumin, immunoglobulins, bovine serum albumin, bovine lactoferrin, and lactoperoxidase, together with other minor components. Different bioactivities have been associated with these proteins. In many cases, caseins and whey proteins act as precursors of bioactive peptides that are released, in the body, by enzymatic pro…

animal structuresAntioxidantmedicine.medical_treatmentProteolysisReview ArticleBiochemistryfluids and secretionsmedicineFood scienceBovine serum albuminMolecular Biologychemistry.chemical_classificationbiologymedicine.diagnostic_testbusiness.industryLactoperoxidasefood and beveragesBiological activityGeneral MedicineAntimicrobialEnzymechemistryBiochemistrybiology.proteinAntibodybusiness
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The deubiquitinase USP11 is a versatile and conserved regulator of autophagy

2021

Autophagy is a major cellular quality control system responsible for the degradation of proteins and organelles in response to stress and damage to maintain homeostasis. Ubiquitination of autophagy-related proteins or regulatory components is important for the precise control of autophagy pathways. Here, we show that the deubiquitinase ubiquitin-specific protease 11 (USP11) restricts autophagy and that KO of USP11 in mammalian cells results in elevated autophagic flux. We also demonstrate that depletion of the USP11 homolog H34C03.2 in Caenorhabditis elegans triggers hyperactivation of autophagy and protects the animals against human amyloid-β peptide 42 aggregation-induced paralysis. USP11…

autophagyhAβ42 human amyloid-β protein 1 to 42Lipid kinase activityPI(3)P phosphatidylinositol-3-phosphatemTORC1BiochemistryCell LineGene Knockout Techniqueschemistry.chemical_compoundubiquitinAnimalsHumansULK1 unc-51-like autophagy activating kinase 1WIPI WD-repeat domain phosphoinositide-interacting proteinPI3KC3-C1Caenorhabditis elegansCaenorhabditis elegans ProteinsmTORC1Molecular BiologyMechanistic target of rapamycinUSP11 ubiquitin-specific protease 11proteostasisAmyloid beta-PeptidesS6K S6 kinasebiologyPhosphatidylinositol 3-phosphateAutophagyDUB deubiquitinaseLFQ label-free quantificationIP immunoprecipitationNHT nonhuman targetingPI3KC3-C1 class III phosphatidylinositol 3-kinase complex ICell BiologyACN acetonitrile amyloid-βNRBF2 nuclear receptor-binding factor 2Peptide FragmentsCell biologydeubiquitinase (DUB)ProteostasischemistryProteotoxicitymTORC1 mechanistic target of rapamycin complex 1biology.proteinAutophagy-Related Protein-1 HomologBSA bovine serum albuminThiolester HydrolasesResearch ArticleJournal of Biological Chemistry
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Thermal aggregation of proteins in presence of metal ions.

2008

The study of the aggregation processes in presence of metal ions is an essential step for understanding the key role of metals in protein-protein and protein-solvent interactions. Indeed, the presence of metal ions can radically change the main features of the standard denaturation/aggregation processes and such effects result to be strongly dependent on the kind of metal and on its concentration. Metal ions have an active role in thermal aggregation and cold set gelation processes. These processes are intrinsically different, but both are based on the proteins ability to form aggregates.

beta-LactoglobulinBovine Serum AlbuminProteins aggregation processeMetal IonConformational changeSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Spectroscopic studies of water-soluble superstructured iron(III) porphyrin. Interaction with the bovine serum albumin protein

2018

Acid-base equilibrium of the “one-face”-hindered sulfonated porphyrin, α5,15-[2,2′(dodecamethyleneoxy),(5-sulfonato)diphenyl]-10,20-bis(2-hydroxy,5-sulfonatophenyl)porphyrinato iron(III), has been ...

biologyAlbumin02 engineering and technology010402 general chemistry021001 nanoscience & nanotechnology01 natural sciencesPorphyrin0104 chemical scienceslaw.inventionchemistry.chemical_compoundWater solublechemistrylawMaterials Chemistrybiology.proteinPhysical and Theoretical ChemistryBovine serum albumin0210 nano-technologyElectron paramagnetic resonanceNuclear chemistryJournal of Coordination Chemistry
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Drug Binding Properties of Tyrosine-Modified Human Serum Albumin

1978

Human serum albumin (HSA) has only a small number of specific binding sites for drugs. There are facts indicating that tyrosine residues may be involved in these binding sites. Thus we modified HSA with tetranitromethan, a reagent specific for tyrosine residues in proteins. As derived from an UV-absorption quotient three albumins with a degree of modification of two, five and eight residues per molecule were obtained. Only for the albumin with eight residues modified a small reduction of ordered secondary structure was found.

biologyChemistryAlbuminSerum albuminPlasma protein bindingHuman serum albuminBiochemistrybiology.proteinmedicineBinding siteTyrosineBovine serum albuminProtein secondary structuremedicine.drug
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