Search results for "Enzyme Assay"

showing 10 items of 155 documents

Kinetics of in vivo inhibition of tissue cathepsin d by pepstatin A

1988

1. 1. We have investigated the kinetics of inhibition of cathepsin D in heart, liver and skeletal muscle of CD-1 mice following administration of 25, 50, 100 and 200 mg/kg i.p. of pepstatin A, a specific inhibitor of this protease. 2. 2. In the liver, a significant inhibition of cathepsin D occurred up to at least 15 days, whereas, in heart and skeletal muscle, this inhibition lasted for a much shorter period of time. 3. 3. These results show that the recovery of enzyme activity to normal values is dose-dependent and that, at the same dose level, marked differences occur in the recovery of enzyme activity in these organ tissues, the liver being the most sensitive one. © 1988.

Pepstatin Amedicine.medical_treatmentPeriod (gene)KineticsCathepsin DBiochemistryCathepsin DMicechemistry.chemical_compoundIn vivoPepstatinsmedicineAnimalsProteasebiologyMusclesMyocardiumSkeletal muscleEnzyme assayKineticsmedicine.anatomical_structureLiverchemistryBiochemistrybiology.proteinFemaleProteinase InhibitorsOligopeptidesPepstatin
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Discovery of benzimidazole-based Leishmania mexicana cysteine protease CPB2.8ΔCTE inhibitors as potential therapeutics for leishmaniasis

2018

Abstract: Chemotherapy is currently the only effective approach to treat all forms of leishmaniasis. However, its effectiveness is severely limited due to high toxicity, long treatment length, drug resistance, or inadequate mode of administration. As a consequence, there is a need to identify new molecular scaffolds and targets as potential therapeutics for the treatment of this disease. We report a small series of 1,2‐substituted‐1H‐benzo[d]imidazole derivatives (9ad) showing affinity in the submicromolar range (Ki = 0.150.69 μM) toward Leishmania mexicanaCPB2.8ΔCTE, one of the more promising targets for antileishmanial drug design. The compounds confirmed activity in vitro against intrace…

BenzimidazoleCell SurvivalIn silicoLeishmania mexicanaAntiprotozoal AgentsDrug Evaluation PreclinicalProtozoan ProteinsDrug resistanceCysteine Proteinase InhibitorsPharmacologyAntileishmanial agents Benzimidazole derivatives Docking studies In silico profiling Leishmania mexicanaCPB2.8 Biochemistry Molecular Medicine01 natural sciencesBiochemistryLeishmania mexicanaCell LineInhibitory Concentration 50chemistry.chemical_compoundCysteine ProteasesDrug DiscoverymedicineHumansAmastigoteLeishmaniasisBiologyEnzyme AssaysPharmacologyBinding Sitesbiology010405 organic chemistryChemistryPharmacology. TherapyOrganic ChemistryHydrogen BondingLeishmaniasisbiology.organism_classificationmedicine.diseaseLeishmaniaProtein Structure Tertiary0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistryChemistryMolecular MedicineBenzimidazolesHuman medicineLeishmania infantumChemical biology and drug design
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Studies on the importance of microsomal epoxide hydrolase in the detoxification of arene oxides using the heterologous expression of the enzyme in ma…

1994

In order to investigate the role of the microsomal epoxide hydrolase (mEH) in the detoxification of arene oxides in the presence of a high endogenous glutathione S-transferase (GST) activity-a situation found in several organs--we expressed the rat mEH cDNA in BHK21 Syrian hamster cells. These cells have high GST activities but contain an extremely low endogenous mEH enzyme activity. We obtained several cell clones which expressed the mEH heterologously, as determined by immunoblotting. The cell clone BHK21-mEH/Mz1 had the highest level of mEH protein. Immunofluorescence showed that the level of expression was almost homogeneous throughout the cell population. Total protein isolated from th…

Cancer ResearchPopulationCell Linechemistry.chemical_compoundCricetinaeMicrosomesAnimalsBenzopyrenesCloning MolecularEpoxide hydrolaseeducationGlutathione TransferaseEpoxide Hydrolaseseducation.field_of_studybiologyGeneral MedicineGlutathioneMolecular biologyEnzyme assayRecombinant ProteinsRatsGlutathione S-transferasechemistryBiochemistryMicroscopy FluorescenceCell cultureMicrosomal epoxide hydrolaseInactivation Metabolicbiology.proteinMicrosomeCarcinogenesis
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Reactions of Flavonoids with o‑Quinones Interfere with the Spectrophotometric Assay of Tyrosinase Activity

2016

Flavonoids are important food components with antioxidant properties and many of them have been described as tyrosinase inhibitors. Oxidation of quercetin, kaempferol, morin, catechin, and naringenin by mushroom tyrosinase and their influence on the oxidation of l-dopa and l-tyrosine was studied. Reaction rates measured spectrophotometrically and by oxygen consumption differed substantially. All tested flavonoids reacted with 4-tert-butyl-o-benzoquinone and/or 4-methyl-o-benzoquinone, although at different rates. These reactions generated products whose UV-vis spectra either overlapped or did not overlap with the spectrum of dopachrome. They therefore strongly influence the kinetic analysis…

0301 basic medicineNaringenino-quinoneAntioxidantAgaricusTyrosinasemedicine.medical_treatmentMorintyrosinase01 natural sciencesFungal Proteins03 medical and health scienceschemistry.chemical_compoundBenzoquinonesmedicineOrganic chemistryenzymatic assay interferenceEnzyme AssaysCatecholMonophenol Monooxygenase010401 analytical chemistryfood and beveragesCatechinGeneral Chemistrycatechol0104 chemical sciencesKinetics030104 developmental biologychemistrySpectrophotometryflavonoidsDopachromeredox exchangeGeneral Agricultural and Biological SciencesKaempferolOxidation-ReductionNuclear chemistryJournal of Agricultural and Food Chemistry
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Heterogeneity of Morquio disease.

1986

Further clinical heterogeneity of Morquio disease, mucopolysaccharidosis IV (MPS IV), is delineated by the observation of a 30-year-old man with unusually mild clinical manifestations. He is 156 cm tall, has comparatively mild skeletal abnormalities and fine corneal deposits. Keratosulfaturia is absent. N-Acetylgalactosamine-6-sulfate (GalNAc-6-S) sulfatase (E.C. 3.1.6.-) was markedly reduced in his fibroblasts. The residual enzyme activity exhibited a pH profile comparable to that of patients with the "classical" form of the disorder. From our observation and a review of the literature it is concluded that Morquio disease can be divided in several subgroups: besides the severe ("classical"…

AdultMalemedicine.medical_specialtyDiseaseMucopolysaccharidosis Type IVAInternal medicineGeneticsmedicineHumansGenetics (clinical)chemistry.chemical_classificationbiologybusiness.industrySulfataseGenetic VariationMucopolysaccharidosis IVFibroblastsHydrogen-Ion Concentrationbeta-GalactosidasePhenotypeEnzyme assayChondroitinsulfatasesEnzymeEndocrinologyPhenotypechemistrybiology.proteinMucopolysaccharidosis IVbusinessNeuraminidaseClinical genetics
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Evaluation of an amino acid residue critical for the specificity and activity of human Gb3/CD77 synthase

2016

Human Gb3/CD77 synthase (α1,4-galactosyltransferase) is the only known glycosyltransferase that changes acceptor specificity because of a point mutation. The enzyme, encoded by A4GALT locus, is responsible for biosynthesis of Gal(α1–4)Gal moiety in Gb3 (CD77, Pk antigen) and P1 glycosphingolipids. We showed before that a single nucleotide substitution c.631C > G in the open reading frame of A4GALT, resulting in replacement of glutamine with glutamic acid at position 211 (substitution p. Q211E), broadens the enzyme acceptor specificity, so it can not only attach galactose to another galactose but also to N-acetylgalactosamine. The latter reaction leads to synthesis of NOR antigens, which are…

0301 basic medicineAcetylgalactosamineMutation MissenseBiochemistryGlycosphingolipidsSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundGb3/CD77 synthaseBiosynthesisCell Line TumorGlycosyltransferaseAspartic acidHumansAsparagineSite-directed mutagenesisMolecular BiologySite-directed mutagenesisbiologyAntigens NuclearGlutamic acidCell BiologyGalactosyltransferasesMolecular biologyEnzyme assayGlutamineP1PK blood group system030104 developmental biologyAmino Acid SubstitutionBiochemistrychemistryGlycopshingolipidsbiology.proteinNOR polyagglutinationOriginal ArticleGlycoconjugate Journal
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Use of Medaka Fish as Vertebrate Model to Study the Effect of Cocoa Polyphenols in the Resistance to Oxidative Stress and Life Span Extension.

2018

Oxidative stress (OS) can induce cell apoptosis and thus plays an important role in aging. Antioxidant foods protect tissues from OS and contribute to a healthier lifestyle. In this study, we described the used of medaka embryos (Oryzias latipes) to study the putative antioxidant capacity of dietary cocoa extract in vertebrates. A polyphenol-enriched cocoa extract regulated the expression of several genes implicated in OS, thereby protecting fish embryos from induced OS. The cocoa extract activated superoxide dismutase enzyme activity in embryos and adult fish tissues, suggesting a common mechanism for protection during embryonic development and adulthood. Furthermore, long-term feeding of …

0301 basic medicineAgingAntioxidantanimal structuresantioxidantEmbryo Nonmammalianmedicine.medical_treatmentOryziasLongevityOryziasmedicine.disease_causecocoa polyphenolsSuperoxide dismutase03 medical and health sciencesbiology.animalmedaka fishBotanymedicinelife span extensionAnimalsSodFlavonoidsCacaobiologyPlant ExtractsSuperoxide DismutaseCocoa ExtractVertebratefood and beveragesGene Expression Regulation DevelopmentalPolyphenolsVitamin K 3EmbryoHydrogen Peroxidebiology.organism_classificationEnzyme assayCell biologyOxidative Stress030104 developmental biologyembryonic structuresDietary Supplementsbiology.proteinFoxOGeriatrics and GerontologyOxidative stressRejuvenation research
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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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Stabilization of anti-leukemic enzyme l-asparaginase by immobilization on polysaccharide levan

2001

Abstract Biologically active fructose polymer levan from Zymomonas mobilis of different molecular mass (75 and 2000 kDa) was covalently coupled to anti-leukemic enzyme Erwinia carotovora l -asparaginase. The method used for the immobilization of the enzyme involved periodate oxidation of the polysaccharide, followed by reductive alkylation. A gentle periodate oxidation of levan (oxidation degree ≤24%) resulted in the highest residual enzyme activity (≥55%). The K m(app.) of glycoconjugates was higher than the K m of native l -asparaginase. The conjugation of l -asparaginase widened the optimum pH range of the enzyme. The electrophoretic mobility in polyacrylamide gel of glycoconjugates obta…

chemistry.chemical_classificationAsparaginaseChromatographybiologyImmobilized enzymeChemistryGlycoconjugateProcess Chemistry and TechnologyPeriodateBioengineeringbiology.organism_classificationBiochemistryZymomonas mobilisCatalysisEnzyme assaychemistry.chemical_compoundEnzymeBiochemistrybiology.proteinPolyacrylamide gel electrophoresisJournal of Molecular Catalysis B: Enzymatic
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Ultra-long-distance running and the liver.

1990

During an ultra-long-distance race (1000 km in 20 days) the influence of running was examined on the enzymes aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (AP), gamma-glutamyl-transferase (GGT), and glutamate dehydrogenase (GLDH) with regard to their release from the liver cells or their induction. Furthermore the liver synthetic capacity was assayed by measuring the enzyme activity of cholinesterase and the concentration of serum albumin during the race. Of the 110 participants, 55 finished the race and only the results of these runners were used in our study. AP increased continuously from day 0 (mean = 102 U/L) to day 19 (mean = 120 U/L). A fivefo…

AdultMalemedicine.medical_specialtySerum albuminPhysical Therapy Sports Therapy and Rehabilitationdigestive systemRunningInternal medicinemedicineHumansOrthopedics and Sports MedicineSerum AlbuminCholinesteraseAgedchemistry.chemical_classificationAnalysis of VariancebiologyLiver cellGlutamate dehydrogenaseAlbuminMiddle Ageddigestive system diseasesEnzyme assayOxygenEnzymeEndocrinologychemistryLiverEnzyme Inductionbiology.proteinPhysical EnduranceAlkaline phosphataseFemaleLiver CirculationInternational journal of sports medicine
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