Search results for "Kinetic"

showing 10 items of 3064 documents

Inhibition of Efavirenz Metabolism by Sertraline and Nortriptyline and Their Effect on Efavirenz Plasma Concentrations.

2015

ABSTRACT Between 22 and 45% of HIV-positive subjects are likely to report symptoms of depression. Considering this background, a potential pharmacokinetic interaction between the nonnucleoside reverse transcriptase inhibitor efavirenz (EFV) and two antidepressants, sertraline (SRT) and nortriptyline (NT), was studied. Rats were administered EFV alone or together with the antidepressants, and changes in the plasma levels and pharmacokinetic parameters of EFV were analyzed. Additional in vitro experiments with rat and human hepatic microsomes were carried out to evaluate the inhibitory effect of SRT and NT on EFV metabolism by determining the formation rate of the major EFV metabolite (8-OH-E…

CyclopropanesMalemedicine.medical_specialtyEfavirenzAnti-HIV AgentsMetaboliteNortriptylinePharmacology030226 pharmacology & pharmacy03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePharmacokineticsIn vivoInternal medicineSertralinemedicineAnimalsHumansPharmacology (medical)Drug Interactions030212 general & internal medicineRats WistarIC50PharmacologyChemistryAntidepressive AgentsBenzoxazinesInfectious DiseasesEndocrinologyAlkynesMicrosomeMicrosomes LiverReverse Transcriptase InhibitorsNortriptylinehuman activitiesDrug metabolismmedicine.drugAntimicrobial agents and chemotherapy
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Cytochrome F as Indicator for the Interaction of the Two Photosystems in the State 1 and State 2

1990

The transition of plants into a State 1 or a State 2 by an excess of PS I or PS II excitation was described by BONAVENTURA and MYERS [1]. Since the time of their investigations fluorometric methods gained increasing importance in analyzing the distribution of energy between the two photosystems [21. It was possible to correlate the altered energy balance to the phosphorylation of LHCII and it’s migration into non-appressed thylakoid membranes [31. However fluorescence measurements can give only indirect evidences that also changes in the activity of the two photosystems are produced by the changed energy distribution. A direct assessment of the photochemical variations during state transiti…

Cytochrome fChemistryThylakoidKineticsBiophysicsQuantum yieldFluorescenceRedoxExcitationPhotosystem
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Phosphorylation of rabbit liver cytochrome P-450 LM2 and its effect on monooxygenase activity

1984

The phosphorylation of rabbit liver microsomal cytochrome P-450 LM2 by catalytic subunit of cyclic AMP-dependent protein kinase (W. Pyerin et al. (1983) Carcinogenesis 4, 573) has now been studied in detail with purified soluble form of cytochrome P-450 as well as with the purified protein incorporated into model membranes. The apparent Km values for P-450 of the phosphorylation reaction in all experimental systems were in a range of 2-8 microM, while the Vmax values were dependent on the state of P-450. Upon phosphorylation, the reconstituted enzyme activities with benzphetamine (N-demethylation) and 7-ethoxycoumarin (O-deethylation) as substrates were reduced to 30-40% of control.

CytochromeProtein subunitBiophysicsBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemmedicineAnimalsPhosphorylationProtein kinase AMolecular Biologychemistry.chemical_classificationbiologyKinaseCell BiologyMolecular biologyKineticsEnzymechemistryBiochemistryPhenobarbitalMicrosomes Liverbiology.proteinMicrosomePhosphorylationRabbitsBenzphetamineProtein Kinasesmedicine.drugBiochemical and Biophysical Research Communications
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Kinetic experiments on the binding of metyrapone to liver microsomes

1969

Kinetic experiments on the inhibition of oxidative microsomal O- and N-demethylations by metyrapone (2-methyl-1, 2-bis(3-pyridyl)-l-propanone, Su 4885) were carried out using mouse liver microsomes as the enzyme source. The model substrates were p-nitroanisole and N-monomethyl-p-nitroaniline. It was shown that the inhibition is competitive. The K i for metyrapone is 0.42 × 10−4 M and for the reduced metabolite of metyrapone 1.15×10−4 M. Their spectral dissooiation constants as determined from difference spectra have almost the same values. From this it is concluded that the degree of inhibition is correlated to the amount of metyrapone bound to cytochrome P-450. Metyrapone does not seem to …

CytochromeStereochemistryMetaboliteMixed Function OxygenasesNitrophenolsMicechemistry.chemical_compoundNon-competitive inhibitionmedicineAnimalsBinding siteBiotransformationPharmacologyAniline CompoundsBinding SitesMetyraponebiologyChemistryProadifenSubstrate (chemistry)General MedicineMetyraponeReceptor–ligand kineticsKineticsBiochemistryMicrosomes LiverMicrosomebiology.proteinCytochromesmedicine.drugNaunyn-Schmiedebergs Archiv f�r Pharmakologie
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Cytochrome c is released in a single step during apoptosis

2005

Release of cytochrome c from mitochondria is a central event in apoptotic signaling. In this study, we utilized a cytochrome c fusion that binds fluorescent biarsenical ligands (cytochrome c-4CYS (cyt. c-4CYS)) as well as cytochrome c-green fluorescent protein (cyt. c-GFP) to measure its release from mitochondria in different cell types during apoptosis. In single cells, the kinetics of cyt. c-4CYS release was indistinguishable from that of cyt. c-GFP in apoptotic cells expressing both molecules. Lowering the temperature by 7 degrees C did not affect this corelease, but further separated cytochrome c release from the subsequent decrease in mitochondrial membrane potential (DeltaPsi(m)). Cyt…

CytochromeUltraviolet RaysGreen Fluorescent ProteinsApoptosisLigandsMembrane PotentialsJurkat CellsCytochrome C1HumansCytochrome c oxidaseEnzyme InhibitorsMolecular BiologyProtein Synthesis InhibitorsMicroscopy VideobiologyTumor Necrosis Factor-alphaCytochrome bCytochrome cTemperatureCytochromes cCytochrome P450 reductaseCell BiologyStaurosporineMitochondriaCell biologyKineticsenzymes and coenzymes (carbohydrates)Coenzyme Q – cytochrome c reductaseDactinomycinbiology.proteinApoptosomeBiomarkersHeLa CellsCell Death & Differentiation
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Subcellular localization of pentachlorophenol 4-monooxygenase in Sphingobium chlorophenolicum ATCC 39723.

2002

Abstract We have studied the subcellular localization of pentachlorophenol 4-monooxygenase (PCP4MO) in Sphingobium chlorophenolicum ATCC 39723 during induction by pentachlorophenol (PCP). Using a monoclonal antibody CL6 specific to the native and recombinant PCP4MO, the enzyme was primarily found soluble as determined by immunoblot and ELISA analyses of cellular fractions. However, the enzyme was observed both in the soluble and membrane-bound forms during induction for 2–4 h, suggesting its translocation out from the cytoplasm. Electron microscopy confirmed that PCP4MO was predominantly present in the cytoplasm at 1 h, whereas at 4 h significant amount was detected also in the membrane and…

CytoplasmBiophysicsBiologyProtein Sorting SignalsBiochemistryMixed Function Oxygenaseschemistry.chemical_compoundBiosynthesisAntibody SpecificityInner membraneMolecular BiologySphingobium chlorophenolicumAlphaproteobacteriachemistry.chemical_classificationAntibodies MonoclonalCell BiologyPeriplasmic spacebiology.organism_classificationSubcellular localizationMolecular biologyImmunohistochemistryPentachlorophenolKineticsEnzymechemistryBiochemistryCytoplasmPeriplasmBiochemical and biophysical research communications
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The Yeast RNA Polymerase II-associated Factor Iwr1p Is Involved in the Basal and Regulated Transcription of Specific Genes

2009

RNA polymerase II (RNA pol II) is a multisubunit enzyme that requires many auxiliary factors for its activity. Over the years, these factors have been identified using both biochemical and genetic approaches. Recently, the systematic characterization of protein complexes by tandem affinity purification and mass spectroscopy has allowed the identification of new components of well established complexes, including the RNA pol II holoenzyme. Using this approach, a novel and highly conserved factor, Iwr1p, that physically interacts with most of the RNA pol II subunits has been described in yeast. Here we show that Iwr1p genetically interacts with components of the basal transcription machinery …

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeBiologyBiochemistryPhosphatesFungal ProteinsGene Expression Regulation FungalTranscription Chromatin and EpigeneticsPromoter Regions GeneticMolecular BiologyRNA polymerase II holoenzymeGeneticsModels Geneticbeta-FructofuranosidaseGeneral transcription factorCell BiologyCell biologyKineticsGene Expression RegulationMicroscopy FluorescenceMutationbiology.proteinTranscription factor II FRNA Polymerase IITranscription factor II ETranscription factor II DCarrier ProteinsTranscription factor II BTranscription factor II AJournal of Biological Chemistry
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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Inhibition of the NKp30 activating receptor by pp65 of human cytomegalovirus.

2005

Human cytomegalovirus, a chief pathogen in immunocompromised people, can persist in a healthy immunocompetent host throughout life without being eliminated by the immune system. Here we show that pp65, the main tegument protein of human cytomegalovirus, inhibited natural killer cell cytotoxicity by an interaction with the activating receptor NKp30. This interaction was direct and specific, leading to dissociation of the linked CD3zeta from NKp30 and, consequently, to reduced killing. Thus, pp65 is a ligand for the NKp30 receptor and demonstrates a unique mechanism by which an intracellular viral protein causes general suppression of natural killer cell cytotoxicity by specific interaction w…

Cytotoxicity ImmunologicHuman cytomegalovirusViral proteinvirusesImmunologyCytomegalovirusReceptors Cell SurfaceBiologymedicine.disease_causeNatural killer cellViral Matrix ProteinsMiceImmune systemmedicineAnimalsHumansImmunology and AllergyReceptors ImmunologicCytotoxicityReceptorCells CulturedMembrane GlycoproteinsNatural Cytotoxicity Triggering Receptor 3virus diseasesPhosphoproteinsmedicine.diseaseVirologyImmunoglobulin Fc FragmentsCell biologyKiller Cells NaturalNatural Cytotoxicity Triggering Receptor 3Kineticsmedicine.anatomical_structureGene Expression RegulationIntracellularProtein BindingNature immunology
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In Vivo Protective Effect of Tumour Necrosis Factor   Against Experimental Infection with Herpes Simplex Virus Type 1

1991

C57BL/6 mice, which differ genetically from other strains by their resistance to herpes simplex virus type 1 (HSV-1) infection, were inoculated intraperitoneally with different doses of tumour necrosis factor alpha (TNF-alpha). Mice pretreated with 100 ng, or even 10 ng, of TNF-alpha showed prolonged survival compared to control mice that were infected with 10(7) p.f.u. of HSV-1. Significant protection was observed in mice injected 4 or 8 h prior to or after HSV-1 inoculation, respectively. Protection was also observed when mice which differed at their H-2 locus were treated with TNF-alpha after infection with HSV-1. Interferon could not be detected in the sera of mice at different time poi…

Cytotoxicity ImmunologicTime FactorsNecrosismedicine.medical_treatmentBiologymedicine.disease_causeVirusCell LineNatural killer cellMiceInterferonIn vivoVirologymedicineAnimalsSimplexvirusMice Inbred BALB CTumor Necrosis Factor-alphaHerpes SimplexVirologyRecombinant ProteinsMice Inbred C57BLKineticsHerpes simplex virusCytokinemedicine.anatomical_structureMice Inbred DBAImmunologyTumor necrosis factor alphaInterferonsmedicine.symptommedicine.drugJournal of General Virology
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