Search results for "Kinetic"

showing 10 items of 3064 documents

Glycogen phosphorylase in fish muscle: demonstration of three interconvertible forms

1990

White skeletal muscle of crucian carp contains a single isoenzyme of glycogen phosphorylase, which was purified approximately 300-fold to a specific activity of approximately 13 mumol.min-1.mg protein-1 (assayed in the direction of glycogen breakdown at 25 degrees C). Tissue extracts of crucian muscle produced three distinct peaks of phosphorylase activity when separated on DEAE-Sephacel. Peaks 1 and 3 were identified, in terms of kinetic properties and by interconversion experiments, as phosphorylase b and a, respectively. Peak 2 was shown to be a phospho-dephospho hybrid. The three interconvertible forms of phosphorylase were purified and shown to be dimeric molecules at 20 degrees C. At …

CarpsPhosphorylasesPhysiologyPhysical ExertionAnesthesia GeneralIsozymeChromatography AffinityGlycogen phosphorylasemedicineAnimalsPhosphorylase aPhosphorylase bPhosphorylationGel electrophoresischemistry.chemical_classificationbiologyChemistryMusclesSkeletal muscleCell BiologyChromatography Ion Exchangebiology.organism_classificationIsoenzymesKineticsmedicine.anatomical_structureEnzymeBiochemistryCrucian carpPhosphorylationSpecific activityAmerican Journal of Physiology-Cell Physiology
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Improved model based on the Weibull distribution to describe the combined effect of pH and temperature on the heat resistance of Bacillus cereus in c…

2003

The effect of pH and temperature on the thermal inactivation of different strains of Bacillus cereus was modeled. Inactivation tests were carried out in carrot broth, following a full factorial design at four levels for temperature (from 90 to 105 degrees C, depending on the strain) and pH (6.2, 5.8, 5.2, and 4.7). Individual inactivation curves were analyzed by applying the Weibull model function (with percent discrepancy close to 20% for most cases), and the effects of pH and temperature on the scale parameter (designated D(beta)) and the shape parameter (beta) were also studied. Temperature and pH did not have a significant effect on the shape parameter (beta). The effect of temperature …

Carrot juiceHot TemperatureBacillus cereusThermodynamicsModels BiologicalMicrobiologyShape parameterBeveragesBacillus cereusWeibull distributionStrain (chemistry)biologybusiness.industryChemistryFactorial experimentHydrogen-Ion Concentrationbiology.organism_classificationDaucus carotaBiotechnologyKineticsCereusFood MicrobiologybusinessScale parameterStatistical DistributionsFood Science
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Study on carvacrol and cinnamaldehyde polymeric films: mechanical properties, release kinetics and antibacterial and antibiofilm activities.

2012

Polyethylene-co-vinylacetate (EVA) films with different concentrations (3.5 wt% and 7 wt%) of essential oil constituents, carvacrol or cinnamaldehyde, were prepared and characterized by mechanical, antibacterial and antibiofilm properties. The incorporation of the compounds into copolymer films affected their elastic modulus, tensile stress and elongation at break. Carvacrol and cinnamaldehyde act as plasticizers which reduce the intermolecular forces of polymer chains, thus improving the flexibility and extensibility of the film. The analysis of the surface characteristics demonstrated that essential oil constituents lowered the contact angle values without causing any remarkable variation…

Carvacrol Cinnamaldehyde Polymeric film Mechanical properties Release kinetic BiofilmStaphylococcus aureusPolymersMechanical propertiesBacterial growthEscherichia coli O157Applied Microbiology and BiotechnologyCinnamaldehydelaw.inventionContact anglechemistry.chemical_compoundlawCarvacrolOrganic chemistryCarvacrolAcroleinEssential oilchemistry.chemical_classificationBiofilmBiofilmPlasticizerFood PackagingGeneral MedicinePolymerListeria monocytogenesAnti-Bacterial AgentsRelease kineticKineticsPolymeric filmchemistryBiofilmsMonoterpenesCymenesCarvacrol; Cinnamaldehyde; Polymeric film; Mechanical properties; Release kinetic; BiofilmCinnamaldehydeBiotechnologyNuclear chemistryApplied microbiology and biotechnology
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A Thermophilic Tetramolecular G-Quadruplex/Hemin DNAzyme.

2017

International audience; The quadruplex-based DNAzyme system is one of the most useful artificial enzymes or catalysts; their unique properties make them reliable alternatives to proteins for performing catalytic transformation. The first prototype of a thermally stable DNAzyme system is presented. This thermophilic DNAzyme is capable of oxidizing substrates at high temperatures (up to 95 degrees C) and long reaction times (up to 18 h at 75 degrees C). The catalytic activity of the DNAzymes were investigated with the standard peroxidase-mimicking oxidation of 2,2'-azino-bis(3-ethylbenzothiozoline-6-sulfonic acid) (ABTS) by H2O2. The step-by-step design of this unique heat-activated G-quadrup…

Catalytic transformationDNAzymeoxidationDeoxyribozymeaptamersspecificityNanotechnologyBiocompatible MaterialsdnainsightsG-quadruplex010402 general chemistry[ CHIM ] Chemical Sciences01 natural sciencesperoxidase-mimicking dnazymesCatalysisCatalysischemistry.chemical_compoundOxidizing agent[CHIM]Chemical SciencesBenzothiazolesthermophilicityComputingMilieux_MISCELLANEOUSPeroxidaseChemistry010405 organic chemistryThermophileperoxidase activityGeneral Chemistry[CHIM.CATA]Chemical Sciences/CatalysisGeneral MedicineDNA CatalyticHydrogen PeroxideCombinatorial chemistry0104 chemical sciencesG-QuadruplexesMethylene BluekineticsHeminactivity enhancementSulfonic AcidsporphyrinOxidation-ReductioncomplexHeminAngewandte Chemie (International ed. in English)
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Natural products as inhibitors of recombinant cathepsin L of Leishmania mexicana.

2015

Cysteine proteinases (cathepsins) from Leishmania spp. are promising molecular targets against leishmaniasis. Leishmania mexicana cathepsin L is essential in the parasite life cycle and a pivotal in virulence factor in mammals. Natural products that have been shown to display antileishmanial activity were screened as part of our ongoing efforts to design inhibitors against the L. mexicana cathepsin L-like rCPB2.8. Among them, agathisflavone (1), tetrahydrorobustaflavone (2), 3-oxo-urs-12-en-28-oic acid (3), and quercetin (4) showed significant inhibitory activity on rCPB2.8 with IC50 values ranging from 0.43 to 18.03 µM. The mechanisms of inhibition for compounds 1–3, which showed Ki values…

Cathepsin LImmunologyLeishmania mexicanaVirulence factorLeishmania mexicanaCathepsin BCathepsin LInhibitory Concentration 50Non-competitive inhibitionparasitic diseasesmedicineBiflavonoidsHumansCathepsinBiological ProductsbiologyGeneral Medicinebiology.organism_classificationLeishmaniaRecombinant ProteinsKineticsInfectious DiseasesMechanism of actionBiochemistrybiology.proteinParasitologyQuercetinmedicine.symptomUncompetitive inhibitorExperimental parasitology
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Divalent Cations Reduce the pH Sensitivity of OmpF Channel Inducing the PKA Shift of Key Acidic Residues

2011

In contrast to the highly-selective channels of neurophysiology employing mostly the exclusion mechanism, different factors account for the selectivity of large channels. Elucidation of these factors is essential for understanding the permeation mechanisms in ion channels and their regulation in vivo. The interaction between divalent cations and a protein channel, the bacterial porin OmpF, has been investigated paying attention to the channel selectivity and its dependence on the solution pH. Unlike the experiments performed in salts of monovalent cations, the channel is now practically insensitive to pH, being anion selective all over the pH range considered. Electrostatic calculations bas…

Cation bindingMolecular modelCations DivalentStatic ElectricityInorganic chemistryBiophysicsPorinsGeneral Physics and AstronomyIonDivalentMagnesiumAmino AcidsPhysical and Theoretical ChemistryTransport iònicIon channelchemistry.chemical_classificationCanals iònicsChemistryHydrogen-Ion ConcentrationPermeationPolyelectrolyteProtein Structure TertiaryKineticsIon channelsThermodynamicsSelectivityProtein BindingBiophysical Journal
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Purification and characterization of two exopolyphosphatases from the marine sponge Tethya lyncurium

1995

Abstract Two exopolyphosphatases (exopolyphosphatase I and II; EC 3.6.1.11) which release orthophosphate from inorganic polyphosphates have been detected and purified for the first time from a marine sponge, Tethya lyncurium . Exopolyphosphatase I has a molecular mass of 45 kDa, a pH optimum of 5.0 and does not require divalent cations for activity, while exopolyphosphatase II has a molecular mass of 70 kDa, a pH optimum of 7.5 and displays optimal activity in the presence of Mg 2+ ions. Final purification of the enzymes could be achieved by affinity chromatography on polyphosphate-modified zirconia. The mode of action of both enzymes was found to be processive. Orthophosphate is the sole p…

Cations DivalentBiophysicsAdenylate kinaseBiochemistryPyrophosphateDivalentchemistry.chemical_compoundPolyphosphatesProtein purificationAnimalsMolecular BiologyExopolyphosphatasechemistry.chemical_classificationChromatographyMolecular massPolyphosphateTemperatureHydrogen-Ion ConcentrationAcid Anhydride HydrolasesPoriferaMolecular WeightKineticsEnzymechemistryBiochemistryAdenylyl Cyclase InhibitorsBiochimica et Biophysica Acta (BBA) - General Subjects
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Mammalian intestinal alkaline phosphatase acts as highly active exopolyphosphatase.

2001

Recent results revealed that inorganic polyphosphates (polyP), being energy-rich linear polymers of orthophosphate residues known from bacteria and yeast, also exist in higher eukaryotes. However, the enzymatic basis of their metabolism especially in mammalian cells is still uncertain. Here we demonstrate for the first time that alkaline phosphatase from calf intestine (CIAP) is able to cleave polyP molecules up to a chain length of about 800. The enzyme acts as an exopolyphosphatase degrading polyP in a processive manner. The pH optimum is in the alkaline range. Divalent cations are not required for catalytic activity but inhibit the degradation of polyP. The rate of hydrolysis of short-ch…

Cations DivalentBiophysicsBiologymedicine.disease_causeBiochemistryDivalentSubstrate SpecificityNitrophenolschemistry.chemical_compoundOrganophosphorus CompoundsStructural BiologyNickelPolyphosphatesmedicineAnimalsMagnesiumneoplasmsMolecular BiologyEscherichia coliEdetic AcidExopolyphosphatasechemistry.chemical_classificationPolyphosphateSubstrate (chemistry)MetabolismCobaltHydrogen-Ion ConcentrationAlkaline PhosphataseMolecular biologydigestive system diseasesAcid Anhydride HydrolasesIntestinesKineticsEnzymechemistryBiochemistryAlkaline phosphataseCattleBiochimica et biophysica acta
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Kinetic and thermodynamic insights into interaction of erlotinib with epidermal growth factor receptor: Surface plasmon resonance and molecular docki…

2020

Abstract Epidermal growth factor receptor (EGFR) plays an important role in cell proliferation at non-small cell lung cancer (NSCLC). Therefore, targeted therapy of cancer via this kind of receptor is highly interested. Small molecule drugs such as erlotinib and gefitinib inhibit EGFR tyrosine kinase and thus suppress cell proliferation. At this paper, erlotinib interaction with EGFR on the cell surface was studied via surface plasmon resonance (SPR) and molecular docking methods. Kinetic parameters indicated that erlotinib affinity toward EGFR was increased through increment of temperature. The thermodynamic analysis showed that van der Waals and hydrogen binding forces play a major role i…

Cell Culture TechniquesQuantitative Structure-Activity RelationshipAntineoplastic Agents02 engineering and technologyMolecular Dynamics SimulationBiochemistry03 medical and health sciencesErlotinib HydrochlorideGefitinibStructural BiologymedicineHumansheterocyclic compoundsEpidermal growth factor receptorSurface plasmon resonanceReceptorneoplasmsMolecular BiologyProtein Kinase Inhibitors030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryCell growthGeneral MedicineSurface Plasmon Resonance021001 nanoscience & nanotechnologySmall moleculerespiratory tract diseasesErbB ReceptorsMolecular Docking SimulationKineticsDocking (molecular)biology.proteinBiophysicsThermodynamicsErlotinib0210 nano-technologymedicine.drugProtein BindingInternational journal of biological macromolecules
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Dynamics of Ca2+ and guanosine 5'-[gamma-thio]triphosphate action on insulin secretion from alpha-toxin-permeabilized HIT-T15 cells.

1994

The time course of Ca2+ and GTP-analogue effects on insulin secretion was investigated in HIT-T15 cells permeabilized with Staphylococcus alpha-toxin. These cells responded to Ca2+ in the range 0.1-10 microM and could be used in a dynamic perifusion system because of the minimal run-down of the secretory response. High Ca2+ (10 microM) elicited a monophasic ATP-dependent stimulation of insulin secretion that reached a peak within 5 min (approximately 20-fold increase) and rapidly decreased during the subsequent 15 min to a plateau remaining above basal rates (0.1 microM Ca2+). The decrease in Ca(2+)-induced insulin secretion with time could not be attributed to decreased capacity to respond…

Cell Membrane PermeabilityGTP'medicine.medical_treatmentStimulationCalcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitorsBiochemistryPiperazinesAdenosine TriphosphateDesensitization (telecommunications)1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineInsulin SecretionGuanosine 5'-O-(3-Thiotriphosphate) - pharmacologyStaphylococcus aureus alpha-toxinInsulinGuanosine Triphosphate - pharmacologyGuanylyl ImidodiphosphateKinasePiperazines - pharmacologyInsulin secretionAdenosine Triphosphate - pharmacologyPermeabilized cellsGuanosine TriphosphateResearch Articlemedicine.medical_specialtyStaphylococcus aureuschemistry.chemical_elementBiologyCalciumGuanylyl Imidodiphosphate - pharmacologyExocytosisCell LineInsulin - secretionInternal medicinemedicine1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - analogs & derivativesSecretionMolecular BiologyInsulinCell BiologyIsoquinolinesATPKineticsEndocrinologyCalcium - pharmacologychemistryIsoquinolines - pharmacologyGuanosine 5'-O-(3-Thiotriphosphate)Type C PhospholipasesCalcium-Calmodulin-Dependent Protein KinasesCalciumType C Phospholipases - pharmacologyGTP
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