Search results for "Pronase"

showing 10 items of 11 documents

Colon bioaccessibility under in vitro gastrointestinal digestion of a red cabbage extract chemically profiled through UHPLC‐Q‐Orbitrap HRMS

2020

Red cabbage is a native vegetable of the Mediterranean region that represents one of the major sources of anthocyanins. The aim of this research is to evaluate the antioxidant capability and total polyphenol content (TPC) of a red cabbage extract and to compare acquired data with those from the same extract encapsulated in an acid-resistant capsule. The extract, which was qualitatively and quantitatively profiled by UHPLC-Q-Orbitrap HRMS analysis, contained a high content of anthocyanins and phenolic acids, whereas non-anthocyanin flavonoids were the less abundant compounds. An in vitro gastrointestinal digestion system was utilized to follow the extract&rsquo

0301 basic medicineAntioxidantPhysiologyAcid‐resistant capsulemedicine.medical_treatmentClinical BiochemistryIn vitro gastrointestinal digestionBioaccessibilityPronaseOrbitrapBiochemistryArticlelaw.invention03 medical and health sciences0404 agricultural biotechnologyfoodNutraceuticallawmedicineUHPLC-Q-Orbitrap HRMSUHPLC‐Q‐Orbitrap HRMSFood scienceacid-resistant capsuleMolecular Biology030109 nutrition & dieteticsRed cabbageChemistrylcsh:RM1-950fungifood and beveragesCapsule04 agricultural and veterinary sciencesCell BiologyMetabolism040401 food sciencefood.foodcarbohydrates (lipids)lcsh:Therapeutics. PharmacologyantioxidantsPolyphenolUHPLC-Q-Orbitrap HRMS.AntioxidantRed cabbage
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Protein-bound tyrosine oxidation, nitration and chlorination by-products assessed by ultraperformance liquid chromatography coupled to tandem mass sp…

2015

Abstract Background Free radicals cause alterations in cellular protein structure and function. Oxidized, nitrated, and chlorinated modifications of aromatic amino acids including phenylalanine and tyrosine are reliable biomarkers of oxidative stress and inflammation in clinical conditions. Objective To develop, validate and apply a rapid method for the quantification of known hallmarks of tyrosine oxidation, nitration and chlorination in plasma and tissue proteins providing a snapshot of the oxidative stress and inflammatory status of the organism and of target organs respectively. Material and Methods The extraction and clean up procedure entailed protein precipitation, followed by protei…

0301 basic medicineHalogenationSwinePhenylalaninePronaseProtein oxidationTandem mass spectrometrymedicine.disease_cause01 natural sciencesBiochemistryAnalytical Chemistry03 medical and health scienceschemistry.chemical_compoundTandem Mass SpectrometryNitrationmedicineAromatic amino acidsAnimalsEnvironmental ChemistryTyrosineSpectroscopyNitratesChromatography010401 analytical chemistryProteins0104 chemical sciences030104 developmental biologyAnimals NewbornchemistryBiochemistryTyrosineOxidation-ReductionOxidative stressChromatography LiquidAnalytica Chimica Acta
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Development of an Analytical Assay for Electrochemical Detection and Quantification of Protein-Bound 3-Nitrotyrosine in Biological Samples and Compar…

2020

Reactive oxygen and nitrogen species (RONS) cause oxidative damage, which is associated with endothelial dysfunction and cardiovascular disease, but may also contribute to redox signaling. Therefore, their precise detection is important for the evaluation of disease mechanisms. Here, we compared three different methods for the detection of 3-nitrotyrosine (3-NT), a marker of nitro-oxidative stress, in biological samples. Nitrated proteins were generated by incubation with peroxynitrite or 3-morpholino sydnonimine (Sin-1) and subjected to total hydrolysis using pronase, a mixture of different proteases. The 3-NT was then separated by high performance liquid chromatography (HPLC) and quantifi…

0301 basic medicinePhysiologyClinical BiochemistryDot blotmitochondrial superoxidePronase030204 cardiovascular system & hematologymedicine.disease_causeBiochemistryHigh-performance liquid chromatographyArticleperoxynitritePeroxynitrite03 medical and health sciences0302 clinical medicineProtein-bound 3-nitrotyrosinemedicineoxidative stressBovine serum albuminMolecular Biologychemistry.chemical_classificationDetection limitReactive oxygen speciesChromatographyHPLC with electrochemical detectionbiologylcsh:RM1-950Cell Biology3. Good health030104 developmental biologylcsh:Therapeutics. PharmacologychemistryOxidative stressbiology.proteinprotein-bound 3-nitrotyrosineOxidative stressEx vivoMitochondrial superoxide
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Evaluation of the proteolysis degree with the o-phthalaldehyde/N-acetyl-L-cysteine reagent

1990

The o-phthalaldehyde/N-acetyl-L-cysteine (OPA-NAC) reagent is applied to the spectrophotometric evaluation of the proteolytic activity of enzymes. The high stability of the OPA-NAC isoindoles makes a strict control of the time of reaction unnecessary. A mathematical expression is proposed to calculate proteolysis degrees, where the absorbance decrease of the OPA-NAC derivative of the protein itself during the hydrolysis process is taken into account. The method is applied to bovine serum albumine, caseine, lysozyme, lactoglobuline and protamine sulphate as substrates, and pronase, papaine, trypsin and chymotrypsin as enzymes.

ChymotrypsinChromatographybiologymedicine.diagnostic_testChemistryProteolysisPronaseTrypsinBiochemistryAnalytical ChemistryO-Phthalaldehydechemistry.chemical_compoundReagentbiology.proteinmedicineLysozymeBovine serum albuminmedicine.drugFresenius' Journal of Analytical Chemistry
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Association of hepatitis Be antigen (HBeAg) with the core of the hepatitis B virus (HBcAg).

2008

— Three substances (pronase E, sodium dodecylsulfate (SDS) and guanidine hydrochloride) with different chemical actions partially convert HBcAg to HBeAg. This process retains the integrity of the HBcAg particle, which was not different between HBcAg subpopulations, and does not generate HBcAg or HBeAg sub-units. DNA polymerase activity was destroyed by SDS and guanidine hydrochloride, but not by pronase E. Serum HBeAg could not be converted into HBcAg, suggesting that this might be an irreversible process. The data are consistent with the assumption that HBcAg and HBeAg are coded for by the same gene (C gene of the HBV-DNA).

DNA polymerasePronaseDNA-Directed DNA Polymerasemedicine.disease_causeGuanidinesHepatitis B Antigenschemistry.chemical_compoundAntigenmedicineHumansHepatitis B e AntigensGuanidineGuanidineHepatitisHepatitis B virusHepatologybiologyChemistryvirus diseasesSodium Dodecyl Sulfatemedicine.diseaseHepatitis BVirologyHepatitis B Core Antigensdigestive system diseasesHBcAgHBeAgPronasebiology.proteinLiver
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A new neuraminic acid derivative and three types of glycopeptides isolated from the Cuvierian tubules of the sea cucumber Holothuria forskali

1973

The Cuvierian tubules of Holothuria forskali Della Chiaje, a sea cucumber found in the Adriatic Sea, were investigated with regard to their carbohydrate moieties. From a Pronase digest of these tubules three types of carbohydrate units were isolated and characterized. 1. A high-molecular-weight glycopeptide fraction was shown to contain sulphated polyfucose, galactosamine, a uronic acid and a previously unknown neuraminic acid derivative. The sulphate was shown by i.r. analysis to be present as an O-ester. The carbohydrate unit was linked O-glycosidically to threonine and serine residues in the polypeptide chain. The hitherto unknown neuraminic acid derivative (Hf-neuraminic acid) was resis…

ElectrophoresisChromatography PaperCarbohydratesUronic acidHydroxylysineBiochemistrychemistry.chemical_compoundSpecies SpecificityNeuraminic acidAnimalsAmino Acid SequenceGlycosidesAmino AcidsThreonineMolecular BiologyFucosechemistry.chemical_classificationHolothuria forskalibiologyGlycopeptidesGlycosideHexosaminesGlycosidic bondCell BiologyHydrogen-Ion ConcentrationSulfuric Acidsbiology.organism_classificationGlycopeptideAmino acidMolecular WeightUronic AcidsBiochemistrychemistryPronaseChromatography GelNeuraminic AcidsChromatography Thin LayerPeptidesEchinodermataBiochemical Journal
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Evidence that C1q, a Subcomponent of the First Component of Complement, is an Fc Receptor of Peritoneal and Alveolar Macrophages

1980

Abstract Guinea pig peritoneal macrophages were cultured for 24 h in the presence of two inhibitors of the biosynthesis of collagen-like molecules such as C1q : 10 -3 M 3,4-dehydroproline or 10 -4 M 2,2′-dipyridyl. Their Fc-receptor activity was measured by rosette formation, using sheep erythrocytes (E) coated with rabbit anti-sheep IgG (EA IgG ). The Fc-receptor activity was decreased by 40 to 70% of control cultures depending on the amount of IgG on the E. The activity of a second receptor on the macrophages, mediating the binding of C3b coated E, was not altered by this treatment. Rat alveolar macrophages were depleted of their Fc-receptor activity by pronase treatment (1.5 mg/ml) in th…

MaleRosette FormationProlineGuinea PigsImmunologyFc receptorReceptors FcPronaseGuinea pigchemistry.chemical_compound22'-DipyridylBiosynthesisComplement C1AnimalsAscitic FluidImmunology and AllergySecretionReceptorIncubationbiologyMacrophagesComplement C3HematologyMolecular biologyRatsReceptors ComplementPulmonary AlveoliMembraneBiochemistrychemistryPronasebiology.proteinFemaleImmunobiology
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Activation of the first component of complement, C1: comparison of the effect of sixteen different enzymes on serum C1.

1983

In this study, the effect of sixteen different enzymes on serum C1 and its subcomponents was investigated. The sixteen enzymes could be divided into three groups. First, enzymes which activate native C1: trypsin (optimal concentration 2.4 x 10(-4) mM); alpha-chymotrypsin (2.3 x 10(3) mM); thrombin (1.0 x 10(-5) mM); plasmin (1.9 x 10(-5) mM); elastase (5.8 x 10(-5) mM); pronase (3.0 x 10(-6) mM). All these enzymes are serine esterase and activate native serum C1 bound to EAC4 at the given concentration within 10 min at 30 degrees C. Furthermore, native C1 inhibited by a pentosanpolysulfoester, Sp54, is unable to undergo the internal activation but can be externally activated by the serine e…

PlasminComplement Activating EnzymesImmunologyGuinea PigsDose-Response Relationship ImmunologicPronaseSerinechemistry.chemical_compoundComplement C1medicineImmunology and AllergyAnimalsHumansTrypsinFibrinolysinComplement Activationchemistry.chemical_classificationPentosan Sulfuric PolyesterbiologyHematologyTrypsinCarboxypeptidaseKineticsEnzymeBiochemistrychemistrybiology.proteinCollagenaseCattleRabbitsLysozymemedicine.drugPeptide HydrolasesImmunobiology
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Regulation of chitin synthase activity inSaccharomyces cerevisiae: Effect of the inhibition of cell division and of synthesis of RNA and protein

1980

The effect of pronase and trypsin on the activation or deactivation (degradation?) of chitin synthase ofSaccharomyces cerevisiae occurs faster in membranous preparations than in toluene-treated cells. When the temperature is raised, the former preparation is deactivated earlier than the latter one. The activity found in growing cells is not modified after inhibition of protein synthesis by cycloheximide or amino acid starvation or by the inhibition of RNA synthesis. It was possible to activate the chitin synthase ofS. cerevisiae cdc 25 grown at 23°C by means of pronase, whereas trypsin had no effect. After the cells were grown at 37°C, chitin synthase could not be activated either with tryp…

chemistry.chemical_classificationCell divisionRNAGeneral MedicinePronaseChitin synthaseCycloheximideBiologyTrypsinApplied Microbiology and BiotechnologyMicrobiologyAmino acidchemistry.chemical_compoundchemistryBiochemistrymedicinebiology.proteinProtein biosynthesismedicine.drugCurrent Microbiology
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Lipodepsipeptides from Pseudomonas syringae are partially proteolyzed and are not absorbed by humans: An in vitro study

2008

There are some concerns about the use of Pseudomonas-based products as biocontrol agents because of the hemolytic activity shown by their metabolites. The effects of Pseudomonas lipodepsipeptides (LDPs) on mammals via ingestion and the LDP degradation during the digestion and intestinal permeability have not been evaluated. In this research, the susceptibility of different LDPs to degradation was assayed with enzymatic gastrointestinal digestion, and intestinal permeability to LDPs was investigated in an in vitro system based on an intestinal cell layer system. Results demonstrated that trypsin and chymotrypsin hydrolyze up to 50% of the various LDPs, and that proteolysis was further increa…

lipodepsipeptidesProteolysisPseudomonas syringaelipodepsipeptides; Pseudomonas syringae; enzymatic digestionPronaseIn Vitro TechniquesPeptides CyclicRisk AssessmentMicrobiologyMicrobiologyenzymatic digestionmedicinePseudomonas syringaeHumansLife SciencePest Control BiologicalIntestinal permeabilitybiologymedicine.diagnostic_testPseudomonasbiology.organism_classificationTrypsinmedicine.diseaseIntestinal AbsorptionBiochemistryConsumer Product SafetyDigestionDigestionFood Sciencemedicine.drugPseudomonadaceaeJournal of Food Protection
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