Search results for "Buffers"

showing 10 items of 53 documents

Physiological HEPES Buffer Proposed as a Calibrator for pH Measurement in Human Blood

1999

Abstract N-(2-hydroxyethyl)-piperazine-N'-2-ethanesulfonic acid, known as HEPES buffer, with p K in the physiological range was studied for use as an alternative to conventional phosphate buffer for the calibration of pH in modern clinical analyzers. In different series of aqueous equimolar HEPES buffer, pH was measured at 37 °C with a capillary glass electrode standardized previously using phosphate, and variations due to changes in total HEPES buffer concentration (0.025 to 0.320 mol/l), and NaCl (0 to 0.250 mol/l) were monitored. For 0.05 equimolar HEPES buffer without NaCl, the pH of 7.362 ± 0.003 (n = 15) obtained coincided well with the reference pH (7.364) from the National Institute…

SodiumClinical BiochemistryAnalytical chemistrySalt (chemistry)chemistry.chemical_elementBuffersSodium ChlorideBuffer (optical fiber)law.inventionchemistry.chemical_compoundlawProhibitinsHumansHEPESchemistry.chemical_classificationAqueous solutionChromatographyBiochemistry (medical)General MedicineBuffer solutionHydrogen-Ion ConcentrationPhosphateGlass electrodechemistryCalibrationHEPESBlood Chemical Analysiscclm
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Mechanisms of endothelial cell swelling from lactacidosis studied in vitro

2000

One of the early sequelae of ischemia is an increase of circulating lactic acid that occurs in response to anaerobic metabolism. The purpose of the present study was to investigate whether lactic acidosis can induce endothelial swelling in vitro under closely controlled extracellular conditions. Cell volume of suspended cultured bovine aortic endothelial cells was measured by use of an advanced Coulter technique employing the “pulse area analysis” signal-processing technique (CASY1). The isosmotic reduction of pH from 7.4 to 6.8 had no effect on cell volume. Lowering of pH to 6.6, 6.4, or 6.0, however, led to significant, pH-dependent increases of cell volume. Swelling was more pronounced …

Sodium-Hydrogen ExchangersPhysiologyIschemia44'-Diisothiocyanostilbene-22'-Disulfonic AcidBuffersPharmacologyAmiloridechemistry.chemical_compoundPhysiology (medical)medicineAnimalsCells CulturedAcidosisBiological TransportSignal Processing Computer-AssistedHydrogen-Ion Concentrationmedicine.diseaseIn vitroCulture MediaLactic acidEndothelial stem cellBicarbonatesmedicine.anatomical_structurechemistryBiochemistryAcidosis LacticCattleEndothelium VascularSwellingmedicine.symptomCardiology and Cardiovascular MedicineHEPESAnaerobic exerciseBlood vesselAmerican Journal of Physiology-Heart and Circulatory Physiology
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Extent of the influence of phosphate buffer and ionic liquids on the reduction of the silanol effect in a C18 stationary phase

2017

The presence of anionic free silanols in the silica-based stationary phases gives rise to broad and asymmetrical peaks when cationic basic compounds are chromatographed using hydro-organic mobile phases. The addition to the mobile phase of a reagent with ionic character prevents the access of analytes to the free silanols, improving the peak shape. The silanol activity can be affected by the buffer concentration and mobile phase pH, factors that are not always considered sufficiently in the literature. In this work, the chromatographic behaviour of three basic β-adrenoceptor antagonists (acebutolol, nadolol and timolol), using mobile phases containing acetonitrile, was examined at different…

Static ElectricityInorganic chemistryIonic LiquidsIonic bonding02 engineering and technologyBuffers01 natural sciencesBiochemistryPhosphatesAnalytical Chemistrychemistry.chemical_compoundPhase (matter)Alkylchemistry.chemical_classificationChromatography Reverse-PhaseChromatography010401 analytical chemistryOrganic ChemistryCationic polymerizationGeneral MedicineReversed-phase chromatographyHydrogen-Ion ConcentrationSilanes021001 nanoscience & nanotechnologyPhosphate0104 chemical sciencesSilanolchemistryIonic liquid0210 nano-technologyJournal of Chromatography A
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Critical parameters for adduct formation of the carcinogen (+)-anti-benzo[a]pyrene-7,8-dihydrodiol 9,10-epoxide with oligonucleotides.

1997

Various parameters relevant for the formation of dG adducts produced in the reaction of individual benzo[a]pyrene diol epoxide (BPDE) stereoisomers with oligonucleotides have been studied. Reaction time, temperature, pH, molar ratio of diol epoxide and oligonucleotide, base sequence, and buffer system were shown to affect the amount of (+)-anti-BPDE dG adducts formed. Optimum experimental conditions for dG adduct formation were different depending on the base sequence context of the oligonucleotide employed [5'-d(CCTATAGATATCC) or 5'-d(CCTATTGCTATCC)]. In general, low temperature to allow a longer reaction time, slightly alkaline Tris-HCl (pH 7.5-8.0) or alkaline phosphate buffer (pH 11), l…

StereochemistryDiol78-Dihydro-78-dihydroxybenzo(a)pyrene 910-oxideBiomedical EngineeringOligonucleotidesPharmaceutical ScienceEpoxideBioengineeringContext (language use)BuffersMedicinal chemistryAdductchemistry.chemical_compoundpolycyclic compoundsPharmacologyOligonucleotideHydrolysisOrganic ChemistryTemperatureHydrogen-Ion ConcentrationchemistryBenzo(a)pyreneCarcinogensPyreneEnantiomerBiotechnologyBioconjugate chemistry
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In vitro degradation of porous PLLA/pearl powder composite scaffolds

2013

Abstract The in vitro degradation behavior of poly- l -lactide (PLLA), PLLA/aragonite pearl powder and PLLA/vaterite pearl powder scaffolds was investigated. The scaffolds were soaked in phosphate buffer solution (PBS) up to 200 days. Scanning electron microscopy (SEM), gel permeation chromatography (GPC), and differential scanning calorimetry (DSC) were used to observe any degradation of the scaffolds. Degradation behaviors such as changes in pH, porosity, bulk density, water absorption, weight loss and mechanical properties were discussed. The results show that a gradual increase of the pH in composite scaffolds can decrease the rate of hydrolysis of PLLA. PLLA/vaterite and PLLA/aragonite…

Time FactorsMaterials scienceAbsorption of waterCompressive StrengthScanning electron microscopePolyestersComposite numberBioengineeringBuffersAbsorptionCalcium CarbonateBiomaterialsGel permeation chromatographyHydrolysischemistry.chemical_compoundDifferential scanning calorimetryVateriteAnimalsTransition TemperatureComposite materialLactideCalorimetry Differential ScanningTissue ScaffoldsWaterHydrogen-Ion ConcentrationMolecular WeightSolutionsChemical engineeringchemistryMechanics of MaterialsMicroscopy Electron ScanningCalciumPowdersPorosityMaterials Science and Engineering: C
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Contribution to the study of the alteration of lipase activity ofCandida rugosa by ions and buffers

1994

A semipurified C. rugosa lipase (LS) has been prepared from commercial lipase (LC) using an economical procedure. The presence of sugars and glycopeptides has been detected in LS and LC. Pure lipase only has covalently bonded sugars. The hydrolysis of olive oil catalyzed by LS and commercial lipase (LC) is sensitive to the presence of cations Na(I), Mg(II), Ca(II), and Ba(II) and to the nature of buffer. Highest enzyme activity is obtained with 0.1M Tris/HCl buffers and the combination of NaCl 0.11M and CaCl2 0.11M. Fluorescence spectroscopy analysis of LC, LS, and both pure isoenzymes lipases A and B, was used to analyze the interaction of the lipase with these effectors. Inorganic cations…

TrisChromatographyMolecular StructurebiologyTriacylglycerol lipaseFluorescence spectrometryBioengineeringLipaseGeneral MedicineBuffersApplied Microbiology and BiotechnologyBiochemistryEnzyme assayCandida rugosachemistry.chemical_compoundHydrolysisSpectrometry FluorescencechemistryIonic strengthCationsbiology.proteinLipaseMolecular BiologyCandidaBiotechnologyApplied Biochemistry and Biotechnology
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Determination of cow’s milk in non-bovine and mixed cheeses by capillary electrophoresis of whey proteins in acidic isoelectric buffers

2000

An improved method for the determination of cow's milk in non-bovine cheese is reported: electrophoresis of whey proteins in acidic, isoelectric buffers. Two background electrolytes (BGEs) have been tested: (i) 50 mM iminodiacetic acid (pH=isoelectric point=2.30 at 25 degrees C), 0.5% hydroxyethylcellulose, 0.1% Tween 20 and 6 M urea (apparent pH 3.1), E=300 V/cm, for the separation of alpha-lactalbumins (alpha-LAs); (ii) a BGE with the same composition, but supplemented with 10% Tween 20, E=450 V/cm, for the fractionation of beta-lactoglobulins (beta-LGs). Surfactants have a discriminating effect on the retention behaviour of the bovine alpha-LA and beta-LG proteins, owing to the different…

Whey proteinCheese ripeningFractionationBuffersSensitivity and SpecificityBiochemistryAnalytical ChemistryCapillary electrophoresisCheeseCaseinAnimalsFood scienceBeta-lactoglobulinSheepChromatographybiologyChemistryGoatsOrganic ChemistryElectrophoresis Capillaryfood and beveragesGeneral MedicineMilk ProteinsMilkWhey ProteinsIsoelectric pointbiology.proteinAlpha-lactalbuminCattleIsoelectric FocusingJournal of Chromatography A
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Effect of buffer nature and concentration on the chromatographic performance of basic compounds in the absence and presence of 1-hexyl-3-methylimidaz…

2019

Abstract In reversed-phase liquid chromatography, the performance for basic compounds is affected by the interaction of the protonated (cationic) species with the anionic free silanols on the alkyl-bonded stationary phases. Using aqueous-organic mobile phases in the absence of additives, the retention may be too high, and the peaks be broad and asymmetric. The performance is improved by addition to the mobile phase of ionic liquids, from which 1-hexyl-3-methylimidazolium chloride ([C6MIm][Cl]) has especially good characteristics. A recent report has also revealed that the use of the phosphate system as buffer, at varying concentration and pH, may have a significant role in the chromatograph…

buffer systemsAcetonitrilesAdrenergic beta-AntagonistsIonic LiquidsProtonationBuffers010402 general chemistry01 natural sciencesBiochemistryChlorideAnalytical Chemistryionic liquidschemistry.chemical_compoundreversed-phase liquid chromatographyBoratesmedicineFormateβ-Adrenoceptor antagonistsChromatography High Pressure LiquidChromatography Reverse-PhaseChromatography010401 analytical chemistryOrganic ChemistryCationic polymerizationImidazolesWatersilanol effectGeneral MedicineReversed-phase chromatographyHydrogen-Ion ConcentrationPhosphate0104 chemical sciencesSilanolchemistryIonic liquidSolventsmedicine.drug
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Application of Imprinted Synthetic Polymers in Binding Assay Development

2000

The first part of the review describes a method for the synthesis of molecularly imprinted polymers for use in binding assays. The method considers the many factors involved that affect the recognition properties of the materials and describes an approach to screening and optimization of these factors. The second part describes the development of binding assays using such polymers. This includes the use of different labels, the effect of solvent and buffer, the scale of the assay (amount of solid polymer), and how these influence the quality of the assay in terms of sensitivity, selectivity, and speed of analysis.

chemistry.chemical_classificationChromatographyChromatographyPolymersLigand binding assayDrug Evaluation PreclinicalMolecular ConformationMolecularly imprinted polymerPolymerBuffersLigandsSensitivity and SpecificityGeneral Biochemistry Genetics and Molecular BiologyPharmaceutical PreparationschemistrySolventsAdsorptionSelectivityMolecular BiologyMethods
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Effects of isoflurane on the Dnase I activity in an isolated enzyme preparation and on the Dnase I-G actin complex

1991

Effects of isoflurane on the DNase I activity in an isolated enzyme preparation and in the DNase I-globular (G) actin complex were investigated. DNase I, DNase I-G actin complex, and G actin were exposed to various (0.2–4.0 vol%) isoflurane concentrations for 180 min. Thereafter, DNase I activity was determined. DNase I activity was inhibited in relation to time and concentration of isoflurane exposure. At concentrations ranging from 0.2 to 1.0 vol% of isoflurane inactive DNase I was activated in the DNase I-G actin complex. The DNase I inhibitor G actin showed a reduced capability to inhibit DNase I following isoflurane exposure. Albumin can inhibit the DNase I inactivation possibly by com…

chemistry.chemical_classificationProtein DenaturationIsofluraneAlbuminAbsorption (skin)BuffersToxicologyMolecular biologyActinschemistry.chemical_compoundEnzymechemistryBiochemistryIsofluranemedicineAnimalsDeoxyribonuclease ICattlePancreasDNAActinDNA Damagemedicine.drugJournal of Biochemical Toxicology
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