Search results for "Oxidase test"

showing 3 items of 53 documents

Synergistic Anticancer Therapy by Ovalbumin Encapsulation-Enabled Tandem Reactive Oxygen Species Generation

2020

Abstract The anticancer efficacy of photodynamic therapy (PDT) is limited due to the hypoxic features of solid tumors. We report synergistic PDT/chemotherapy with integrated tandem Fenton reactions mediated by ovalbumin encapsulation for improved in vivo anticancer therapy via an enhanced reactive oxygen species (ROS) generation mechanism. O2 .− produced by the PDT is converted to H2O2 by superoxide dismutase, followed by the transformation of H2O2 to the highly toxic .OH via Fenton reactions by Fe2+ originating from the dissolution of co‐loaded Fe3O4 nanoparticles. The PDT process further facilitates the endosomal/lysosomal escape of the active agents and enhances their intracellular deliv…

inorganic chemicalsNanomedicines | Hot PaperOvalbuminmedicine.medical_treatmentRadicalsynergisticcisplatinPhotodynamic therapyAntineoplastic Agents010402 general chemistry01 natural sciencesCatalysisSuperoxide dismutasechemistry.chemical_compoundMicemedicineAnimalsHumansResearch Articleschemistry.chemical_classificationCisplatinReactive oxygen speciesOxidase testPhotosensitizing Agentsbiology010405 organic chemistryFenton reactionsDrug SynergismGeneral MedicineGeneral ChemistryhypoxicEndocytosis0104 chemical sciencesOvalbuminchemistryphotodynamic therapybiology.proteinBiophysicsMCF-7 CellsReactive Oxygen SpeciesNicotinamide adenine dinucleotide phosphatemedicine.drugResearch Article
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Preparation of a dansylated fibrate, a new fluorescent tool to study peroxisome proliferation. Effect on hepatic-derived cell lines.

1997

The synthesis of a dansylated fibrate (DNS-X) has been performed in order to identify the cellular affinity sites of peroxisome proliferators and to establish the subcellular localization of such molecules. DNS-X has been obtained by coupling the dansy1 chloride with the amine resulting from the bezafibrate alkaline hydrolysis. The purified DNS-X has been further characterized by spectrum analysis (UV-Vis, fluorescence, [1H]/[13C]-NMR and mass). At 250 microM and incubated for 48 h with the rat hepatic derived cells (Fao cells), DNS-X stimulates 12-fold the palmitoyl-CoA oxidase, a peroxisome proliferation marker enzyme. This increase is comparable to the one obtained with well known peroxi…

medicine.drug_classPeroxisome ProliferationFibrateBiochemistryMicrobodiesCell Linechemistry.chemical_compoundmedicineTumor Cells CulturedAnimalsHumanschemistry.chemical_classificationDansyl CompoundsOxidase testBezafibratefungiDansyl chlorideGeneral MedicineSubcellular localizationRatsEnzymeBiochemistrychemistryLiverCiprofibrateBezafibratemedicine.drugBiochimie
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In vitro free radical scavenging capacity of thyroid hormones and structural analogues.

2001

It was reported that thyroid hormones decreased Cu(2+)-induced low-density lipoprotein (LDL) oxidation in vitro. Here, we investigated free radical scavenging capacities of thyroid hormones (3,5,3'-tri-iodo-L-thyronine (T(3)), thyroxine (T(4)) and 3,3',5'-tri-iodo-L-thyronine (rT(3))) and structural analogues (L-thyronine (T(0)), 3,5,3'tri-iodothyroacetic acid (TA(3)) and 3,5,3',5'-tetra-iodothyroacetic acid (TA(4))), using three different models of free radical generation. T(0), T(3) and TA(3) slowed down production of conjugated diene and thiobarbituric acid-reactive substances during LDL oxidation by 2,2'-azobis-[2-amidinopropane] (water-soluble), whereas rT(3), T(4) and TA(4) had practi…

medicine.medical_specialtyThyroid HormonesTriiodothyronine ReverseEndocrinology Diabetes and MetabolismRadicalMedicinal chemistryThiobarbituric Acid Reactive Substanceschemistry.chemical_compoundEndocrinologyInternal medicinemedicineHumansOxidase testAnalysis of VarianceTriiodothyronineSuperoxideThyroidElectron Spin Resonance SpectroscopyFree Radical ScavengersThiobarbituratesIn vitroLipoproteins LDLThyroxinemedicine.anatomical_structureEndocrinologychemistryBiochemistryTriiodothyronineOxidation-ReductionHormoneLipoproteinThe Journal of endocrinology
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