Search results for "Assay"

showing 10 items of 2241 documents

Isolierung und charakterisierung einer cholinkinase aus Phaseolus vulgaris L.-Keimlingen

1977

Summary The enzyme choline kinase (ATP: Choline phosphotransferase E.C. 2.7.1.32) was extracted and partially purified from hypocotyl hooks of Phaseolus vulgaris L. seedlings. K m -value and pH-dependence of the activity were determined. The amount of enzyme activity in extracts depended on light conditions used for plant growth. Etiolated seedlings showed much lower enzyme levels than those grown in white light. Blue and red light conditions decreased enzyme levels below dark values. The in vitro enzyme activity was influenced by inhibitors and growth regulators. The enzyme activity was stimulated by Atropine, 2-Chloroethylammoniumchloride (Cycocel) and Gibberellic acid and was inhibited b…

chemistry.chemical_classificationCholine kinasebiologyChemistryGeneral Medicinebiology.organism_classificationEnzyme assayHypocotylPhosphotransferasechemistry.chemical_compoundEnzymeBiochemistrybiology.proteinCholinePhaseolusGibberellic acidZeitschrift für Pflanzenphysiologie
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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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The second component of human complement: Detection of two hemolytic forms in plasma by pH Variation

1988

The second component of human complement (C2) in pseudoglobulin prepared from normal plasma eluted as a single peak at high conductivity (30 mS) and pH 4.5 from the cationic exchangers S-Sepharose or Mono S in the Fast Protein Liquid Chromatography (FPLC) System. The C2 was stable at pH 4.5 and 0 degrees C if enzyme inhibitors were used and the pH was raised to 6.0 after elution from the columns. After rechromatography on Mono S in the FPLC System at the median isoelectric point of 5.5 or pH 6.0, the C2 eluted as two distinct hemolytic forms: the first peaked at 16 mS, the second at 30 mS. The two forms of C2 did not correlate with the allotypic variant of C2 in individual, normal human pla…

chemistry.chemical_classificationChromatographyElutionImmunologySize-exclusion chromatographyComplement C4Enzyme-Linked Immunosorbent AssayFast protein liquid chromatographyHematologyComplement C1 Inactivator ProteinsComplement C2Hydrogen-Ion ConcentrationChromatography Ion ExchangeHemolysisComplement factor Bchemistry.chemical_compoundIsoelectric pointEnzymeBiochemistrychemistryAlternative complement pathwayHumansImmunology and AllergySodium dodecyl sulfateImmunobiology
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Analysis of kynurenine transaminase activity in Drosophila by high performance liquid chromatography

1991

Abstract A sensitive assay for kynurenine transaminase activity (E.C. 2.6.1.7) based on rapid separation of the reaction product by high performance liquid chromatography (HPLC) has been developed. Drosophila sordidula extracts have been assayed by this new method and this is the first time that kynurenine transaminase activity has been demonstrated in Drosophila . The method of assay developed can be extended to any other organism. Kynurenine and 3-hydroxykynurenine were both used as substrates, and they were transaminated to kynurenic acid and xanthruenic acid, respectively. HPLC is used to separate and quantitate these reaction products from all other components in the reaction mixture. …

chemistry.chemical_classificationChromatographybiologyBiochemistryHigh-performance liquid chromatographyEnzyme assayTransaminaseAmino acidchemistry.chemical_compoundKynurenic acidBiochemistrychemistryInsect Sciencebiology.proteinSpecific activityPyruvic acidMolecular BiologyKynurenineInsect Biochemistry
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Thermal inactivation at high temperatures and regeneration of green asparagus peroxidase

2019

A spectrophotometric method was developed for determining the peroxidase activity of green asparagus in small samples. The optimum conditions for the analysis in the cuvette were 45 mM of H2O2 36 mM of guaiacol, and pH 7. The method can be used to determine enzyme activity at up to two decimal reductions. A study was performed of the regeneration and inactivation kinetics of the enzyme when heated between 90 and 125°C. Regenerated asparagus peroxidase reached its maximum activity after being stored 6 days at 25°C. The regenerated enzyme followed first-order inactivation kinetics, showing an Ea = 13.62 kcal/mol and k100°C = 2.07 min-1.

chemistry.chemical_classificationChromatographybiologyChemistryKineticsfood and beveragesbiology.organism_classificationMicrobiologyEnzyme assayCuvettechemistry.chemical_compoundEnzymeBiochemistrybiology.proteinAsparagusGuaiacolEnzyme kineticsFood SciencePeroxidase
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Isolation and characterization of a chlorogenic acid esterase from Aspergillus niger.

1980

Abstract The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum were 6.5 and 45 °C respectively. Divalent cations were not required for the enzyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. The Km-value is 0.70 mᴍ chlorogenic acid, the molecular weight 240000. The described enzyme is specific for chlorogenic acid. On the other hand a typical unspecific esterase like the pig liver esterases does not split…

chemistry.chemical_classificationChromatographybiologyIsoelectric focusingSwineAspergillus nigerbiology.organism_classificationEsteraseGeneral Biochemistry Genetics and Molecular BiologyEnzyme assayIsoenzymesMolecular Weightchemistry.chemical_compoundHydrolysisKineticsEnzymeChlorogenic acidchemistryLiverCaffeic acidbiology.proteinAnimalsAspergillus nigerCarboxylic Ester HydrolasesZeitschrift fur Naturforschung. Section C, Biosciences
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Purification and characterization of leucine aminopeptidase from kidney bean cotyledons

1992

A leucine aminopeptidase (EC 3,4,11.1) was purified from cotyledons of resting kidney beans (Phaseolus vulgaris L. cv. Processor) by acidic extraction, ammonium sulfate fractionation and chromatography on DEAE-Sephacel, Sephacryl S-300, Mono Q HPLC and Superose HPLC columns. The yield of the 317-fold purified enzyme was 9%. On gel filtrations on Sephacryl S-300 and Superose HPLC the elution volumes of the enzyme corresponded to an M, of 360 000. The enzyme gave one band on native gel electrophoresis and an electrophoretic titration in an immobilized pH gradient gave a single curve with a pI of 4.8. Two bands were observed in an SDS-gel electrophoresis with Mr values of 58 000 and 60 000 bot…

chemistry.chemical_classificationChromatographybiologyPhysiologyCell BiologyPlant ScienceGeneral MedicineAminopeptidaseHigh-performance liquid chromatographyEnzyme assayDithiothreitolSuperosechemistry.chemical_compoundEnzymechemistryBiochemistryGeneticsbiology.proteinImmobilized pH gradientLeucinePhysiologia Plantarum
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Effects of protein on retention of ADH enzyme activity encapsulated in trehalose matrices by spray drying

2008

The retention of the enzymatic activity of alcohol dehydrogenase (ADH) on spray drying was examined under various drying conditions. Trehalose was used in the formulation of feed stocks for the spray drying. The retention of ADH activity was dependent on the concentration of ADH in the feed solution. The addition of other proteins, such as bovine serum albumin and β-lactoglobulin, exhibited an additional improvement of the retention of ADH activity. The inlet and outlet temperature of the drying air was another key factor for the enzyme activity on the spray drying. The surface morphology of the spray-dried particle was changed drastically with the addition of proteins.

chemistry.chemical_classificationChromatographybiologyTrehaloseEnzyme assaychemistry.chemical_compoundEnzymechemistrySpray dryingbiology.proteinBovine serum albuminhormones hormone substitutes and hormone antagonistsFood ScienceAlcohol dehydrogenaseJournal of Food Engineering
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Luminometric sub-nanoliter droplet-to-droplet array (LUMDA) and its application to drug screening by phase I metabolism enzymes.

2012

Here we show the fabrication of the Luminometric Sub-nanoliter Droplet-to-droplet Array (LUMDA chip) by inkjet printing. The chip is easy to be implemented and allows for a multiplexed multi-step biochemical assay in sub-nanoliter liquid spots. This concept is here applied to the integral membrane enzyme CYP3A4, i.e. the most relevant enzymatic target for phase I drug metabolism, and to some structurally-related inhibitors.

chemistry.chemical_classificationChromatographytechnology industry and agricultureBiomedical EngineeringAssayBioprintingDrug Evaluation PreclinicalBioengineeringGeneral ChemistryMicroarray AnalysisBiochemistryMembraneEnzymechemistryLuminescent MeasurementsCytochrome P-450 CYP3ANanotechnologyBiochipBiosensorInkjet printingDrug metabolismLab on a chip
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Deoxyribonucleases in Herpes simplex Virus Type 1 and 2 Infected Primary Rabbit Kidney Cells

1980

Abstract In primary rabbit kidney cells infected with herpes simplex virus four different neutral deoxyribonuclease activities can be detected by means of the deoxyribonuclease assay in DNA-containing polyacrylamide gels following their separation by discelectrophoresis. The method is suitable to follow independently the change in each activity of the different enzymes using only about 5 × 105 cells for each assay during the time-course of infection. Under these conditions one enzyme activity is constant, two disappear while the activity of a fourth one present only in infected cells, increases.

chemistry.chemical_classificationDeoxyribonucleasesbiologyChemistryDeoxyribonucleaseCell Transformation ViralKidneymedicine.disease_causeVirologyGeneral Biochemistry Genetics and Molecular BiologyEnzyme assayKineticsHerpes simplex virusEnzymemedicinebiology.proteinRabbit kidneyAnimalsSimplexvirusRabbitsDeoxyribonucleasesCells CulturedZeitschrift für Naturforschung C
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