Search results for "lcsh:Animal biochemistry"

showing 5 items of 5 documents

Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis.

2008

Abstract Background The interconversion of two important energy metabolites, 3-hydroxybutyrate and acetoacetate (the major ketone bodies), is catalyzed by D-3-hydroxybutyrate dehydrogenase (BDH1: EC 1.1.1.30), a NAD+-dependent enzyme. The eukaryotic enzyme is bound to the mitochondrial inner membrane and harbors a unique lecithin-dependent activity. Here, we report an advanced purification method of the mammalian BDH applied to the liver enzyme from jerboa (Jaculus orientalis), a hibernating rodent adapted to extreme diet and environmental conditions. Results Purifying BDH from jerboa liver overcomes its low specific activity in mitochondria for further biochemical characterization of the e…

lcsh:Animal biochemistryMESH : AgedMESH : RodentiaMESH: RodentiaMESH: Base SequenceBiochemistryMESH: Lipid PeroxidationMESH : Information ServicesAntigen-Antibody ReactionsMESH: Health EducationEpitopesMESH: OrganizationsMESH: LibrariesMESH: Antigen-Antibody Reactionslcsh:QD415-436MESH: AnimalsMESH : OrganizationsMESH : Physician's RoleMESH: Bacterial ProteinsImmunosorbent Techniqueschemistry.chemical_classificationMESH: Conserved SequenceMethodology ArticleMESH : Computer Communication NetworksMESH: Chromatography AffinityMESH : Pseudomonas aeruginosaMESH : Chromatography AffinityMESH : Immunosorbent TechniquesMESH: Ethnic GroupsMESH : Ethnic GroupsMESH: EpitopesMESH : Patient SatisfactionMESH : United StatesMESH: MitochondriaMESH : Antigen-Antibody ReactionsMolecular Sequence DataMESH : Hydroxybutyrate DehydrogenaseMESH: Sequence AlignmentRodentiaMESH: Information ServicesMESH : Epitopeslcsh:BiochemistryMESH : Mitochondrial MembranesBacterial ProteinsMESH : Conserved SequenceComplementary DNAMESH : LibrariesMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Immunosorbent TechniquesMESH: Molecular Sequence DataMESH: HumansMESH : Consumer ParticipationMESH : HumansMESH: AdultMESH: Patient SatisfactionMESH: Hydroxybutyrate DehydrogenaseMESH: Consumer ParticipationchemistryLipid PeroxidationMESH: FemaleMESH: LiverMESH : Sequence Analysis DNAMESH: Continental Population GroupsMESH: Sequence Analysis DNAMESH : Molecular Sequence DataDehydrogenaseChromatography AffinityMESH: Mitochondrial MembranesMESH: Antibodies BacterialMESH : Bacterial ProteinsMESH : FemaleMESH: Computer Communication NetworksConserved SequenceMESH: AgedbiologyMESH : Lipid PeroxidationMESH : Sequence AlignmentMESH: Physician's RoleMESH : AdultAntibodies BacterialMitochondriaAmino acidLiverBiochemistryMitochondrial MembranesPseudomonas aeruginosaMESH: Pseudomonas aeruginosaMESH : MitochondriaMESH : Mass MediaMESH: Mass MediaMESH : MaleHydroxybutyrate DehydrogenaseAffinity chromatographyMESH : Health Education[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: United StatesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Antibodies Bacteriallcsh:QP501-801Jaculus orientalisMESH : Continental Population GroupsBase SequenceMESH : LiverSequence Analysis DNAbiology.organism_classificationMolecular biologyMESH: MaleEnzymePolyclonal antibodiesbiology.proteinMESH : Base SequenceNAD+ kinaseMESH : AnimalsSequence Alignment
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Characterization of sulfhydryl oxidase from Aspergillus tubingensis

2017

Background Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. Results The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initia…

0301 basic medicineentsyymitBOVINE-MILKThioredoxin reductaselcsh:Animal biochemistryBiochemistrySubstrate Specificitychemistry.chemical_compoundNonribosomal peptide synthesisEnzyme Stabilitylcsh:QD415-436DisulfidesDISULFIDE BONDSPeptide Synthaseschemistry.chemical_classificationbiologyGliotoxinChemistrynonribosomal peptide synthesisHydrogen-Ion ConcentrationGlutathioneFAMILYSOXSglutathione oxidationhomesienetAspergillusBiochemistrySENSITIVITYsecreted sulfhydryl oxidaseOxidoreductasesResearch ArticleDithiol oxidaseCofactorlcsh:Biochemistry03 medical and health sciencesNonribosomal peptideNATURAL-PRODUCTSoksidoreduktaasitBIOSYNTHESISlcsh:QP501-801Molecular Biologysecondary metabolismPURIFICATIONIDENTIFICATION030102 biochemistry & molecular biologyCXXC-MOTIFGlutathioneNIGERluonnonaineet030104 developmental biologyEnzymedithiol oxidasebiology.protein1182 Biochemistry cell and molecular biologyAspergillus tubingensisSecreted sulfhydryl oxidaseSecondary metabolismGlutathione oxidationCysteineBMC Biochemistry
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Molecular cloning, gene structure and expression profile of two mouse peroxisomal 3-ketoacyl-CoA thiolase genes

2004

Abstract Background In rats, two peroxisomal 3-ketoacyl-CoA thiolase genes (A and B) have been cloned, whereas only one thiolase gene is found in humans. The aim of this study was thus to clone the different mouse thiolase genes in order to study both their tissue expression and their associated enzymatic activity. Results In this study, we cloned and characterized two mouse peroxisomal 3-ketoacyl-CoA thiolase genes (termed thiolase A and B). Both thiolase A and B genes contain 12 exons and 11 introns. Using RNA extracted from mouse liver, we cloned the two corresponding cDNAs. Thiolase A and B cDNAs possess an open reading frame of 1272 nucleotides encoding a protein of 424 amino acids. In…

Molecular Sequence Datalcsh:Animal biochemistryGene Expressionexpérimentation animalesourislcsh:BiochemistryMiceFenofibratePeroxisomesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyTissue Distributionlcsh:QD415-436Amino Acid SequenceRNA MessengerCloning Molecularlcsh:QP501-801adn complémentaireBase Sequencegèneactivité enzymatiquemammifèreBIOLOGIE MOLECULAIREAcetyl-CoA C-AcyltransferasefoieGene Componentsprotéinegénie génétiqueclonageResearch Articleexpression des gènesBMC Biochemistry
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Surgical implantation of electronic tags does not induce medium-term effect: insights from growth and stress physiological profile in two marine fish…

2020

Abstract Background Telemetry applied to aquatic organisms has recently developed greatly. Physiological sensors have been increasingly used as tools for fish welfare monitoring. However, for the technology to be used as a reliable welfare indicator, it is important that the tagging procedure does not disrupt fish physiology, behaviour and performance. In this communication, we share our medium-term data on stress physiological profile and growth performance after surgical tag implantation in two important marine fish species for European aquaculture, the sea bream (Sparus aurata) and the European sea bass (Dicentrarchus labrax). Results Blood samples after surgical tag implantation (46 day…

0106 biological sciencesComputer Networks and CommunicationsPopulationlcsh:Animal biochemistryZoologyWelfareBiologyStress01 natural sciencesMedium termAccelerometer tags Aquaculture Dicentrarchus labrax Sparus aurata Stress Telemetry WelfareFish physiologyAquacultureSparus auratalcsh:QH540-549.5TelemetryDicentrarchus labraxSea basseducationInstrumentationlcsh:QP501-801Electronic tagseducation.field_of_studybusiness.industry010604 marine biology & hydrobiologyMarine fishAccelerometer tags04 agricultural and veterinary sciencesbiology.organism_classificationSignal Processing040102 fisheries0401 agriculture forestry and fisheriesAnimal Science and ZoologyDicentrarchuslcsh:EcologybusinessAnimal Biotelemetry
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Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver and brain tissues of jerboa (Jaculus o…

2003

Abstract Background Jerboa (Jaculus orientalis) is a deep hibernating rodent native to subdesert highlands. During hibernation, a high level of ketone bodies i.e. acetoacetate (AcAc) and D-3-hydroxybutyrate (BOH) are produced in liver, which are used in brain as energetic fuel. These compounds are bioconverted by mitochondrial D-3-hydroxybutyrate dehydrogenase (BDH) E.C. 1.1.1.30. Here we report, the function and the expression of BDH in terms of catalytic activities, kinetic parameters, levels of protein and mRNA in both tissues i.e brain and liver, in relation to the hibernating process. Results We found that: 1/ In euthemic jerboa the specific activity in liver is 2.4- and 6.4- fold high…

MaleBDH: D-3-hydroxybutyrate dehydrogenaseAcetoacetateBlotting Westernlcsh:Animal biochemistryBrainRodentiaBlotting NorthernCatalysisJerboa: <it>Jaculus orientalis</it>Mitochondrialcsh:BiochemistryHydroxybutyrate DehydrogenaseKineticsLiverHibernationJerboa: Jaculus orientalisKetone bodiesAnimalslcsh:QD415-436RNA Messengerlcsh:QP501-801Research ArticleBOH : D-3-hydroxybutyrateBMC Biochemistry
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