Search results for "Hydroxybutyrate Dehydrogenase"

showing 10 items of 13 documents

Alkylation at the active site of the D-3-hydroxybutyrate dehydrogenase (BDH), a membrane phospholipid-dependent enzyme, by 3-chloroacetyl pyridine ad…

1997

The structure of the rat liver's D-3-hydroxybutyrate dehydrogenase (BDH) active site has been investigated using an affinity alkylating reagent, the 3-chloroacetyl pyridine adenine dinucleotide (3-CAPAD). This NAD+ analogue reagent strongly inactivates the enzyme following a concentration- and time-dependent process with a stoichiometry of approximately 1. The reagent reacts at the coenzyme binding site as revealed by the efficient protection by NADH. The effect of 3-CAPAD is stronger with the enzyme into its natural membrane environment than with the lipid-free purified apoBDH or with the reconstituted apoBDH-mitochondrial phospholipid complex. The pH-dependent effect on the inactivation p…

AlkylationStereochemistryAffinity labelMitochondria LiverDehydrogenaseBiochemistryHydroxybutyrate DehydrogenaseMembrane LipidsAnimalsCoenzyme bindingCysteineBinding sitePhospholipidsBinding SitesAffinity labelingMolecular StructurebiologyChemistryActive siteAffinity LabelsGeneral MedicineNADRatsReagentLinear Modelsbiology.proteinNAD+ kinaseBiochimie
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Purification and characterization of the ?-β-hydroxybutyrate dehydrogenase from dromedary liver mitochondria

2001

Abstract d -β-Hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30), a membrane enzyme, has been purified to homogeneity from dromedary ( Camelus dromedarius ) liver mitochondria. Our new purification method consisted of the solubilization of mitochondrial membranes by Triton X 100 and purification of BDH by two steps: DEAE-Sephacel and Phenyl-Sepharose. The molecular mass of the enzyme subunit size was 67 kDa. The purified enzyme is recognized by anti rat liver mitochondrial BDH antibodies. Furthermore, BDH activity was absolutely dependent upon phospholipids. BDH is also characterized by specific enzymatic parameters: an optimum pH of approximately 8 for the oxidation reaction, and approximat…

CamelusPhysiologyProtein subunitBlotting WesternMitochondria LiverDehydrogenaseMitochondrionBiochemistryHydroxybutyrate Dehydrogenasechemistry.chemical_compoundEnzyme StabilityAnimalsMolecular BiologyPhospholipidschemistry.chemical_classificationChromatographyMolecular massTemperatureHydrogen-Ion ConcentrationChromatography Ion ExchangeDissociation constantKineticsMembraneEnzymechemistryBiochemistryTriton X-100Hydrophobic and Hydrophilic InteractionsComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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Sensitivity of liver metabolism in jerboa (Jaculus orientalis) to ciprofibrate, a peroxisome proliferator.

2009

International audience; Ciprofibrate is a well-known drug used to normalize lipid parameters and fibrinogen in atherosclerosis patients. In laboratory rodents such as rats or mice, ciprofibrate exhibits peroxisome proliferator activity. However, to date, no clear alterations or side effects caused by ciprofibrate have been noted in humans. In order to further investigate such possible relationships, we studied the effects of sustained ciprofibrate treatment in jerboas (Jaculus orientalis). In these rodents, ciprofibrate does not induce hepatomegaly or promote liver cell DNA replication, confirming that this species more closely resembles humans than do rats or mice. The jerboas were treated…

Cancer Researchmedicine.medical_specialtyD-3-hydroxybutyrate dehydrogenaseDehydrogenaseBiochemistryJaculus orientalischemistry.chemical_compoundciprofibrateantioxidant enzymesInternal medicineGeneticsmedicine[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biologyclinical enzymesMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biologysubcellular markerbiologyLiver cellPeroxisomeMalondialdehydeEndocrinologyOncologychemistryCatalasebiology.proteinKetone bodiesMolecular MedicineNAD+ kinaseCiprofibratemedicine.drug
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Characterization of two d-β-hydroxybutyrate dehydrogenase populations in heavy and light mitochondria from jerboa (Jaculus orientalis) liver

2005

Mitochondrial membrane-bound and phospholipid-dependent D-beta-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30), a ketone body converting enzyme in mitochondria, has been studied in two populations of mitochondria (heavy and light) of jerboa (Jaculus orientalis) liver. The results reveal significant differences between the BDH of the two mitochondrial populations in terms of protein expression, kinetic parameters and physico-chemical properties. These results suggest that the beta-hydroxybutyrate dehydrogenases from heavy and light mitochondria are isoform variants. These differences in BDH distribution could be the consequence of cell changes in the lipid composition of the inner mitochon…

Gene isoformHEPESchemistry.chemical_classificationbiologyPhysiologyMitochondria LiverRodentiaDehydrogenaseMitochondrionbiology.organism_classificationBiochemistryMolecular biologyHydroxybutyrate DehydrogenaseKineticschemistry.chemical_compoundEnzymeBiochemistrychemistryKetone bodiesAnimalsInner mitochondrial membraneMolecular BiologyJaculus orientalisComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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Prehibernation and hibernation effects on the D-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orient…

2007

The D-3-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30) from liver jerboa (Jaculus orientalis), a ketone body converting enzyme in mitochondria, in two populations of mitochondria (heavy and light) has been studied in different jerboa states (euthermic, prehibernating and hibernating). The results reveal: (1) important variations between states in terms of ketones bodies, glucose and lipid levels; (2) significant differences between the BDH of the two mitochondrial populations in term of protein expression and kinetic properties. These results suggest that BDH leads an important conformational change depending on the physiological state of jerboa. This BDH structural change could be the c…

HibernationMESH: RatsMESH : HibernationMESH : Hydroxybutyrate DehydrogenaseMESH : RodentiaMESH: RodentiaFluorescent Antibody TechniqueMitochondria LiverRodentiaDehydrogenaseMitochondrionBiochemistryMESH : PhospholipidsHydroxybutyrate DehydrogenaseHibernation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimalsMESH: Animals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyInner mitochondrial membraneMESH: Fluorescent Antibody TechniqueJaculus orientalis[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyPhospholipidsMESH: Phospholipidschemistry.chemical_classificationMESH: KineticsbiologyMESH : RatsGeneral MedicineMetabolismbiology.organism_classificationRatsMESH: Hydroxybutyrate DehydrogenaseKineticsMESH : Fluorescent Antibody TechniqueEnzymechemistryBiochemistryMESH : Mitochondria LiverKetone bodiesMESH: Hibernationsense organsMESH : AnimalsMESH : KineticsMESH: Mitochondria Liver
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Post-transcriptional analysis of rat mitochondrial D-3-hydroxybutyrate dehydrogenase control through development and physiological stages.

1991

Abstract The nuclear encoded mitochondrial D -3-hydroxybutyrate dehydrogenase (BDH) is synthesized in the cytosal as a larger precursor. This membrane enzyme which requires lecithin for activity plays an essential role in energy metabolism as a ketone bodies-converting enzyme. A cDNA clone of the rat liver enzyme encompassing an antigenic determinant peptide has been isolated after immunoscreening of a λ gt11 expression library. The nucleotide sequence of this 279-base cDNA insert contains a single open reading frame of 93 amino-acids, which represents about a third of the mature enzyme. Amino-acid sequence analysis predicts a hydrophobic stretch of 29 amino-acids long which probably functi…

MaleAgingBlotting WesternMolecular Sequence DataBiologyGene Expression Regulation EnzymologicEnzyme activatorHydroxybutyrate DehydrogenaseComplementary DNAImmunoscreeningGene expressionAnimalsAmino Acid SequenceCloning MolecularRNA Processing Post-TranscriptionalGenechemistry.chemical_classificationMessenger RNASex CharacteristicsBase SequenceEstradiolRats Inbred StrainsCell BiologyGeneral MedicineDNABlotting NorthernEmbryo MammalianMolecular biologyDietary FatsMitochondriaRatsOpen reading frameEnzymeBiochemistrychemistryOrgan SpecificityFemaleCorticosteroneBiology of the cell
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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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Action of metyrapone on the redox state of free nicotinamide-adenine dinucleotide and on oxygen consumption of perfused rat livers and isolated mitoc…

1971

Metyrapone [2-methyl-1,2-bis-(3-pyridyl)-1-propanone] in a concentration of 5 mM increased the lactate/pyruvate ratio and theΒ-hydroxybutyrate/ acetoacetate ratio in the perfusion fluid of the isolated rat liver by a factor of 6 indicating a considerable shift in the ratio of free [NAD]/[NADH] in both the cytoplasmic and the mitochondrial compartment. Oxygen uptake of the isolated liver was decreased to about one half. The onset of the inhibitory effect on the respiration of the isolated organ was immediate. The inhibition lasted for at least 1 h.

Malemedicine.medical_specialtychemistry.chemical_elementHydroxybutyratesMitochondria LiverNicotinamide adenine dinucleotideIn Vitro TechniquesOxygenRedoxAcetoacetatesElectron Transportchemistry.chemical_compoundHydroxybutyrate DehydrogenaseOxygen ConsumptionInternal medicineRespirationmedicineAnimalsPyruvatesPharmacologyMetyraponeChemistryGeneral MedicineCompartment (chemistry)MetyraponeNADRatsPerfusionKineticsEndocrinologyBiochemistryLiverCytoplasmSpectrophotometryDepression ChemicalLactatesNAD+ kinasemedicine.drugFerrocyanidesPolarographyNaunyn-Schmiedebergs Archiv fur Pharmakologie
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Enzym-histochemische Studien am cervicalen Dr�senfeld des Uterus

1972

Durch enzym-histochemische Untersuchungen an Cervices soll Einblick in den Stoffwechsel des cervicalen Drusenfeldes gewonnen werden. Hierfur wurden insbesondere die Enzyme des Glucosestoffwechsels, der Fettsaureoxydation, des Pentosephosphatstoffwechsels, des Citronensaurecyclus sowie des NADH- und NADPH-Diaphorese-Systems und des Aminosaurestoffwechsels untersucht. Die einheitliche Nachweistechnik erlaubt in Form eines Art Screening-Tests eine Information uber die vorhandenen Aktivitaten der einzelnen Enzyme, wobei — abgesehen von einem Enzym des Glucosestoffwechsels, namlich der Alkoholdehydrogenase und des Aminosaurestoffwechsels, der Glutamatdehydrogenase — alle Fermente nachgewiesen we…

business.industryGlucosephosphate dehydrogenaseObstetrics and GynecologyMedicineGlycerolphosphate DehydrogenaseL-Lactate dehydrogenaseGeneral MedicineHydroxybutyrate dehydrogenasebusinessMolecular biologyArchiv f�r Gyn�kologie
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Interaction of the mitochondrial membrane D-3-hydroxybutyrate dehydrogenase with fluorescent phospholipids

1993

Norbert Latruffe l ,I, Boubker Nasser ‘, Claude Morpain 3, Jiirgen Zirkel 4, Michael Seiter 4, Bernard Laude 3 and Wolfgang Trommer 4 ’ Laboratoire de Biobgie Mol&laire et Cellulaire, Universite’ de Bourgogne, Fact& des Sciences Mirande, BP 138, 21004 D@on Cedex (France) 2 Laboratoire de Biochimie &A CNRS 531) and 3 Laboratoire de Chimie Organique, Universite’ de Franche-Comte 25030 Besaqon Cedex (France) 4 Fachbereich Chemie, Universitiit Kaiserslautem, D 6750 Kaiserslautem (Germany)

chemistry.chemical_classificationBiophysicsPhospholipidMitochondrionBiologyMitochondrial carrierFluorescenceMolecular biologychemistry.chemical_compoundEnzymeBiochemistrychemistryElectrochemistryPhysical and Theoretical ChemistryD-3-Hydroxybutyrate DehydrogenaseInner mitochondrial membraneBranched-chain alpha-keto acid dehydrogenase complexBioelectrochemistry and Bioenergetics
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