Search results for "Pyruvate"

showing 10 items of 134 documents

Messenger RNA of the large subunit of ribulose-1,5-bisphosphate carboxylase from Chlamydomonas reinhardi. Isolation and properties.

1979

Polysomes specifically synthesizing the large subunit of ribulose-1,5-bisphosphate carboxylase were isolated from Chlamydomonas reinhardi cells by the indirect immunoprecipitation method. Electrophoretic analysis showed that the immunoprecipitated polysomes were of chloroplast origin. The mRNA coding for the large subunit which was purified from immunoprecipitated polysomes migrated at the 19-S position on sucrose density gradients, and its molecular weight was estimated to be 7.3 x 10(5) by acid-urea/agarose gel electrophoresis. The mRNA was translated in vivo with a cell-free protein-synthesizing system derived from Escherichia coli to give full-length large-subunit polypeptides.

Messenger RNARibulose 15-bisphosphateImmunoprecipitationCarboxy-LyasesProtein subunitRibulose-Bisphosphate CarboxylaseChlamydomonasChlamydomonasBiologybiology.organism_classificationBiochemistryMolecular biologyPyruvate carboxylaseMolecular Weightchemistry.chemical_compoundBiochemistrychemistryPolysomePolyribosomesProtein BiosynthesisAgarose gel electrophoresisEscherichia coliRNA MessengerEuropean journal of biochemistry
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A New Nuclear Function of the Entamoeba histolytica Glycolytic Enzyme Enolase: The Metabolic Regulation of Cytosine-5 Methyltransferase 2 (Dnmt2) Act…

2009

Cytosine-5 methyltransferases of the Dnmt2 family function as DNA and tRNA methyltransferases. Insight into the role and biological significance of Dnmt2 is greatly hampered by a lack of knowledge about its protein interactions. In this report, we address the subject of protein interaction by identifying enolase through a yeast two-hybrid screen as a Dnmt2-binding protein. Enolase, which is known to catalyze the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), was shown to have both a cytoplasmatic and a nuclear localization in the parasite Entamoeba histolytica. We discovered that enolase acts as a Dnmt2 inhibitor. This unexpected inhibitory activity was antagonized by…

MethyltransferaseQH301-705.5ImmunologyEnolaseProtozoan ProteinsPolymerase Chain ReactionMicrobiologyEntamoeba histolyticaTwo-Hybrid System TechniquesGenetics and Genomics/EpigeneticsVirologyGeneticsImmunoprecipitationDNA (Cytosine-5-)-MethyltransferasesMicrobiology/ParasitologyBiology (General)Molecular BiologyMolecular Biology/DNA MethylationCell Nucleuschemistry.chemical_classificationbiologyEntamoeba histolyticaInfectious Diseases/Protozoal InfectionsMethylationRC581-607biology.organism_classificationTRNA MethyltransferasesEnolase 2EnzymechemistryBiochemistryPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationParasitologyImmunologic diseases. AllergyNuclear localization sequenceResearch ArticlePLoS Pathogens
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Structural and functional consequences of the replacement of proximal residues Cys172 and Cys192 in the large subunit of ribulose-1,5-bisphosphate ca…

2008

Proximal Cys(172) and Cys(192) in the large subunit of the photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae and higher plants. Mutation of Cys(172) has been shown to affect the redox properties of Rubisco in vitro and to delay the degradation of the enzyme in vivo under stress conditions. Here, we report the effect of the replacement of Cys(172) and Cys(192) by serine on the catalytic properties, thermostability and three-dimensional structure of Chlamydomonas reinhardtii Rubisco. The most striking effect of the C172S substitution was an 11% increase in the specificity factor when compared wi…

Models Molecularinorganic chemicalsOxygenaseRibulose-Bisphosphate CarboxylaseProtein subunitSpecificity factorChlamydomonas reinhardtiiCrystallography X-RayBiochemistryCatalysischemistry.chemical_compoundEnzyme StabilityAnimalsCysteineMolecular BiologyBinding SitesRibulose 15-bisphosphatebiologyfungiRuBisCOTemperaturefood and beveragesCell Biologybiology.organism_classificationLyaseMolecular biologyProtein Structure TertiaryPyruvate carboxylaseKineticsProtein SubunitsBiochemistrychemistryMutationbiology.proteinChlamydomonas reinhardtiiBiochemical Journal
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c-erbB-2 expression in small-cell lung cancer is associated with poor prognosis.

2001

Small-cell lung cancer (SCLC) carries a bad prognosis despite good initial response to chemotherapy. It is therefore important to identify molecular markers that influence survival as potential new therapeutic targets. In our study, expression of the tyrosine kinase c-erbB-2 (HER2/neu) receptor in tumor tissues of 107 consecutive newly diagnosed patients with primary SCLC was quantified using a monoclonal antibody directed against the c-terminal domain of c-erbB-2. A clear-cut positive expression of c-erbB-2 was observed in 13% of patients. Surprisingly, c-erbB-2 was an independent prognostic factor (RR = 2.16; p = 0.014) when a proportional-hazard model was adjusted to stage (limited vs. e…

OncologyMaleCancer Researchmedicine.medical_specialtyPathologyLung NeoplasmsTime FactorsReceptor ErbB-2medicine.medical_treatmentSmall-cell carcinomaDisease-Free SurvivalSex FactorsInternal medicinemedicineCarcinomaHumansCarcinoma Small CellLung cancerneoplasmsAgedProportional Hazards ModelsChemotherapyPerformance statusL-Lactate DehydrogenaseProportional hazards modelbusiness.industryAge FactorsCancerAntibodies MonoclonalMiddle Agedmedicine.diseasePrognosisImmunohistochemistryProtein Structure TertiaryTreatment OutcomeOncologyPhosphopyruvate HydrataseImmunohistochemistryFemalebusinessInternational journal of cancer
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Detection and Differential Diagnosis of Prekallikrein Deficiency: Genetic Study of New Families and Systematic Review of the Literature

2018

Abstract Introduction. Prekallikrein (PK) and high-molecular-weight kininogen (HK) deficiencies are ultra-rare, autosomal-recessive defects of the contact system caused by biallelic mutations in the KLKB1 and KNG1 genes, respectively. Since affected subjects do not manifest a bleeding phenotype, a correct diagnosis is essential to prevent the administration of prohemostatic agents or plasma and to avoid delay of surgery. We describe a new case of PK deficiency identified at UMC Mainz. In addition, we performed a systematic review of the literature in order to i) collect blood material for genetic studies of reported PK deficient cases lacking this information, and ii) perform a comprehensiv…

Oncologymedicine.medical_specialtyMutationHematologymedicine.diagnostic_testbusiness.industryImmunologyPrekallikreinCell BiologyHematologymedicine.diseasemedicine.disease_causeCompound heterozygosityBioinformaticsBiochemistryHexokinase deficiencyInternal medicineMedicineDifferential diagnosisbusinessPyruvate kinase deficiencyGenetic testingScience meets clinical practice
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Mutation of the oxaloacetate decarboxylase gene of Lactococcus lactis subsp. lactis impairs the growth during citrate metabolism

2007

 ; Aims: Citrate metabolism generates metabolic energy through the generation of a membrane potential and a pH gradient. The purpose of this work was to study the influence of oxaloacetate decarboxylase in citrate metabolism and intracellular pH maintenance in relation to acidic conditions. Methods and Results: A Lactococcus lactis oxaloacetate decarboxylase mutant [ILCitM (pFL3)] was constructed by double homologous recombination. During culture with citrate, and whatever the initial pH, the growth rate of the mutant was lower. In addition, the production of diacetyl and acetoin was altered in the mutant strain. However, our results indicated no relationship with a change in the maintenanc…

Oxaloacetic AcidATP citrate lyaseCarboxy-LyasesCITRATE METABOLISMIntracellular pHMolecular Sequence DataDiacetylACIDE LACTIQUEApplied Microbiology and BiotechnologyCitric Acidchemistry.chemical_compoundLACTIC ACID BACTERIAOxaloacetic acidCitrate synthaseBacteriological TechniquesBase SequencebiologyOXALOACETATE DECARBOXYLASEAcetoinLactococcus lactisGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationLactococcus lactis[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyOxaloacetate decarboxylaseBiochemistrychemistryGenes BacterialFermentationMutationINTRACELLULAR PHFood Microbiologybiology.proteinGenetic EngineeringCitric acidPhosphoenolpyruvate carboxykinaseBiotechnologyJournal of Applied Microbiology
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Redox regulation of enzymatic activity and proteolytic susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase fromEuglena gracilis.

1992

The activity of ribulose-1,5-bisphosphate carboxylase/oxygenase fromEuglena gracilis decays steadily when exposed to agents that induce oxidative modification of cysteine residues (Cu(2+), benzofuroxan, disulfides, arsenite, oxidized ascorbate). Inactivation takes place with a concomitant loss of cysteine sulfhydryl groups and dimerization of large subunits of the enzyme. 40% activity loss induced by the vicinal thiol-reagent arsenite is caused by modification of a few neighbor residues while the almost complete inactivation achieved with disulfides is due to extensive oxidation leading to formation of mixed disulfides with critical cysteines of the protein. In most cases oxidative inactiva…

OxygenaseCell BiologyPlant ScienceGeneral MedicineGlutathioneBiochemistryDithiothreitolPyruvate carboxylasechemistry.chemical_compoundchemistryBiochemistryCystamineCysteamineThioredoxinCysteinePhotosynthesis research
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Cysteines 449 and 459 modulate the reduction-oxidation conformational changes of ribulose 1.5-bisphosphate carboxylase/oxygenase and the translocatio…

2006

The role of cysteines 449 (Cys449) and 459 (Cys459) from the large subunit (LS) of ribulose 1-5-bisphosphate carboxylase/oxygenase (Rubisco) in the reduction-oxidation (redox) regulation of the enzyme was assessed by site-directed mutagenesis of these residues and chloroplast transformation of Chlamydomonas reinhardtii. In vitro studies indicated that mutations C449S, C459S or C449S/ C459S do not affect the activity and proteolytic susceptibility of the enzyme in the reduced state. However, when oxidized, the mutant enzymes differed from the wild type (WT), showing an increased resistance to inactivation and, in the case of the double mutant (DM), an altered structural conformation as refle…

OxygenaseProtein ConformationPhysiologyRibulose-Bisphosphate CarboxylaseBlotting WesternChlamydomonas reinhardtiiPlant ScienceBiologychemistry.chemical_compoundCysteinechemistry.chemical_classificationRibulose 15-bisphosphateRibuloseCell MembraneRuBisCOWild typebiology.organism_classificationPyruvate carboxylaseProtein TransportEnzymeBiochemistrychemistryMutagenesis Site-Directedbiology.proteinElectrophoresis Polyacrylamide GelOxidation-ReductionPlant, Cell and Environment
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Increased susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatments

1990

The susceptibility of the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolysis by trypsin, chymotrypsin, proteinase K, and papain is enhanced by oxidative treatments including spontaneous oxidation of cysteines. Proteinases exhibit a high specificity for the oxidized inactive form of the carboxylase, cleaving its large subunit. Treatment of the inactive enzyme with dithiothreitol results in partial recovery of both carboxylase activity and resistance to proteolysis. This behavior may explain the specific degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase that occurs in vivo during leaf senescence.

OxygenaseTime FactorsRibulose-Bisphosphate CarboxylaseProteolysisBiophysicsBiochemistryDithiothreitolchemistry.chemical_compoundEnzyme StabilitymedicineCysteineMolecular Biologychemistry.chemical_classificationChymotrypsinRibulose 15-bisphosphatebiologymedicine.diagnostic_testHydrolysisPlantsTrypsinPyruvate carboxylaseEnzymechemistryBiochemistrybiology.proteinOxidation-ReductionPeptide Hydrolasesmedicine.drugArchives of Biochemistry and Biophysics
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Regional cerebral blood flow and regional metabolism in cold induced oedema.

1973

24 hours following a cold induced oedema in cats rCBF was measured in the lesion area, the bluish stained cortex immediately adjacent to the lesion, a cortical area remote from the lesion, and in the contralateral uninjured hemisphere. Thereafter the brain was frozen and the respective tissue areas were removed and analyzed for water and electrolyte content as well as metabolite concentrations. It seems, that in the neighbourhood of a local lesion at least 3 different brain regions can be differentiated with regard to their characteristic pattern of data. In non-oedematous regions either hyperaemia or hypoaemia could be observed. In areas with local brain oedema rCBF was reduced inversely p…

Pathologymedicine.medical_specialtyBrain EdemaPhosphocreatineMicrocirculationLesionHyperaemiachemistry.chemical_compoundAdenosine TriphosphateIschemiaCortex (anatomy)medicineAnimalsHypoxiaPyruvatesCerebrospinal FluidDiminutionCATSbusiness.industrySodiumBrainAnatomyWater-Electrolyte BalanceAdenosine MonophosphateAdenosine DiphosphateCold Temperaturemedicine.anatomical_structurechemistryCerebral blood flowRegional Blood FlowInjections IntravenousCatsLactatesPotassiumSurgeryNeurology (clinical)medicine.symptombusinessActa neurochirurgica
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