Search results for "Threitol"

showing 10 items of 29 documents

From strong to fragile glass formers: secondary relaxation in polyalcohols.

2002

We have studied details of the molecular origin of slow secondary relaxation near T(g) in a series of neat polyalcohols by means of dielectric spectroscopy and (2)H NMR. From glycerol to threitol, xylitol, and sorbitol the appearance of the secondary relaxation changes gradually from a wing-type scenario to a pronounced beta peak. It is found that in sorbitol the dynamics of the whole molecule contributes equally to the beta process, while in glycerol the hydrogen bond forming OH groups remain rather rigid compared to the hydrogens bonded to the carbon skeleton.

Magnetic Resonance SpectroscopyHydrogen bondSpectrum AnalysisGeneral Physics and AstronomyNuclear magnetic resonance spectroscopyXylitolchemistry.chemical_compoundCrystallographySugar AlcoholschemistryProton NMRRelaxation (physics)MoleculeSorbitolSorbitolGlassThreitolXylitolPhysical review letters
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Disulfide-crosslinked hyaluronan-gelatin hydrogel films: a covalent mimic of the extracellular matrix for in vitro cell growth

2003

A new disulfide crosslinking method was developed for the preparation of blended hyaluronan (HA)-gelatin hydrogels to form a synthetic, covalently linked mimic of the extracellular matrix (ECM). The HA and gelatin were chemically modified using 3,3′-dithiobis(propionic hydrazide) (DTP). After reduction with dithiothreitol (DTT), the thiol derivatives of HA (HA-DTPH) and gelatin (gelatin-DTPH) were obtained and characterized. To minimize interference with biological function, the degree of substitution of HA-DTPH and gelatin-DTPH was kept below 50%. Solutions of HA-DTPH and gelatin-DTPH in varying blends (20%, 40%, 60%, 80% gelatin) were prepared in 1% w/v NaCl and crosslinked by disulfide b…

Magnetic Resonance SpectroscopyTime FactorsBiocompatible MaterialsSodium ChlorideGelatinHydrogel Polyethylene Glycol DimethacrylateDithiothreitolCell growthMicechemistry.chemical_compoundHyaluronic acidDisulfidesHyaluronic Acidchemistry.chemical_classificationMice Inbred BALB CBiomaterialHydrogels3T3 CellsMethylgalactosidesExtracellular MatrixCross-Linking ReagentsMechanics of MaterialsCovalent bondSelf-healing hydrogelsThiolCell DivisionBiotechnologyfood.ingredientMaterials scienceCell SurvivalBiomedical EngineeringBiophysicsHyaluronoglucosaminidaseBioengineeringmacromolecular substancesIn Vitro TechniquesHydrazideBiomaterialsDisulfidefoodPolymer chemistryCell AdhesionAnimalsSulfhydryl Compoundstechnology industry and agricultureFibroblastsBiomaterialDithiothreitolModels ChemicalchemistryCeramics and CompositesGelatinPolystyrenesBiomaterials
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Beneficial effects of dithiothreitol on relative levels of glutathione S-transferase activity and thiols in oocytes, and cell number, DNA fragmentati…

2006

We analyzed the effect of in vitro aging of mouse oocytes in the presence of dithiothreitol (DTT) on relative levels of glutathione S-transferase (GST) activity and thiols in oocytes, and cell number, DNA fragmentation and cellular allocation to the inner cell mass (ICM) and trophectoderm (TE) lineage at the blastocyst stage. Ovulated oocytes from gonadotropin primed hybrid female mice of 6-8 weeks of age were aged in vitro in the presence of 0, 5, 50, or 500 microM DTT for 6 hr prior to insemination. Relative levels of GST activity and thiols in oocytes were determined by confocal laser scanning microscopy, DNA fragmentation using a single-step TUNEL method, and cell allocation to the ICM …

MaleDNA FragmentationFertilization in VitroBiologyDithiothreitolchemistry.chemical_compoundMiceGeneticsmedicineInner cell massAnimalsPropidium iodideBlastocystSulfhydryl Compoundsreproductive and urinary physiologyGlutathione TransferaseTUNEL assayCell BiologyGlutathioneMolecular biologyIn vitroMice Inbred C57BLDithiothreitolmedicine.anatomical_structureBlastocystchemistryembryonic structuresMice Inbred CBAOocytesDNA fragmentationFemaleDevelopmental BiologyMolecular reproduction and development
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ALDH-2 deficiency increases cardiovascular oxidative stress--evidence for indirect antioxidative properties.

2007

Abstract Mitochondrial aldehyde dehydrogenase (ALDH-2) reduces reactive oxygen species (ROS) formation related to toxic aldehydes; additionally, it provides a bioactivating pathway for nitroglycerin. Since acetaldehyde, nitroglycerin, and doxorubicin treatment provoke mitochondrial oxidative stress, we used ALDH-2−/− mice and purified recombinant human ALDH-2 to test the hypothesis that ALDH-2 has an indirect antioxidant function in mitochondria. Antioxidant capacity of purified ALDH-2 was comparable to equimolar doses of glutathione, cysteine, and dithiothreitol; mitochondrial oxidative stress was comparable in C57Bl6 and ALDH-2−/− mice after acute challenges with nitroglycerin or doxorubi…

Mitochondrial ROSAntioxidantmedicine.medical_treatmentBiophysicsAldehyde dehydrogenaseAcetaldehydeMitochondrionPharmacologymedicine.disease_causeBiochemistryCardiovascular SystemModels BiologicalAntioxidantschemistry.chemical_compoundMiceNitroglycerinmedicineAnimalsHumansCysteineMolecular Biologychemistry.chemical_classificationReactive oxygen speciesbiologyDose-Response Relationship DrugAldehyde Dehydrogenase MitochondrialAcetaldehydeCell BiologyGlutathioneAldehyde DehydrogenaseGlutathioneMitochondriaMice Inbred C57BLDithiothreitolOxidative StresschemistryBiochemistryDoxorubicincardiovascular systembiology.proteinReactive Oxygen SpeciesOxidative stressBiochemical and biophysical research communications
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Nuclease activity of [Cu(sulfathiazolato)2(benzimidazole)2]2MeOH. Synthesis, properties and crystal structure

2002

The [Cu(sulfathiazolato)(2)(benzimidazole)(2)]2MeOH complex has been synthesised and characterised. It crystallises in the monoclinic system, space group C1c1, with unit cell dimensions a=18.829(7) A, b=12.206(3) A, c=17.233(5) A, alpha=90.06(2) degrees, beta=97.28(3) degrees, gamma=90.21(3) degrees and Z=4. The geometry around the copper(II) ion is intermediate between tetrahedral and square planar. The complex produces cleavage of plasmid pUC18 in presence of reducing agents. The efficiency of cleavage reaction of the title compound with pUC18 and with different reducing agents follows the order ascorbate-H(2)O(2)>ascorbate>MPA>dithiothreitol>H(2)O(2).

Models MolecularBenzimidazoleSpectrophotometry InfraredReducing agentMolecular Conformationchemistry.chemical_elementCrystal structureCrystallography X-RayCleavage (embryo)BiochemistryDithiothreitolInorganic ChemistryStructure-Activity Relationshipchemistry.chemical_compoundSulfathiazoleOrganometallic CompoundsGroup 2 organometallic chemistrySulfathiazolesDeoxyribonucleasesMethanolElectron Spin Resonance SpectroscopyCopperCrystallographychemistryBenzimidazolesCopperPlasmidsMonoclinic crystal systemJournal of Inorganic Biochemistry
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Redox signaling in acute pancreatitis

2015

Acute pancreatitis is an inflammatory process of the pancreatic gland that eventually may lead to a severe systemic inflammatory response. A key event in pancreatic damage is the intracellular activation of NF-κB and zymogens, involving also calcium, cathepsins, pH disorders, autophagy, and cell death, particularly necrosis. This review focuses on the new role of redox signaling in acute pancreatitis. Oxidative stress and redox status are involved in the onset of acute pancreatitis and also in the development of the systemic inflammatory response, being glutathione depletion, xanthine oxidase activation, and thiol oxidation in proteins critical features of the disease in the pancreas. On th…

NecrosisGSH reduced glutathioneSTAT3 signal transducer and activator of transcription 3ERK extracellular signal-regulated kinasesClinical BiochemistryCCK cholecystokininTRAFs TNF receptor associated factorsReview ArticleIκB kinasePharmacologymedicine.disease_causeBiochemistrySHP small heterodimer partnerSTIM1 stromal interaction molecule 1chemistry.chemical_compoundHATs histone acetyltransferasesMedicineASK1GCL glutamate cysteine ligaseTNF-α tumor necrosis factor alphaIKK IκB kinaseNOS nitric oxide synthaseAcute inflammationHIF hypoxia inducible factorlcsh:QH301-705.5NF-κB nuclear factor kappa BDAMPs damage-associated molecular pattern moleculeslcsh:R5-920biologyGSSG oxidized glutathioneNF-kappa BNLRs nucleotide-binding oligomerization domain (NOD) like receptorsTRADD tumor necrosis factor receptor type 1-associated DEATH domain proteinTRPC3 transient receptor potential channel 3VEGF vascular endothelial growth factorGlutathioneTNFR tumor necrosis factor receptorHMGB1 high-mobility group Box 1 proteinIP3R inositol 145-trisphosphate receptor type 3VCAM-1 Vascular Cell adhesion protein 1Acute DiseaseJNK c-Jun N-terminal kinaseAcute pancreatitisTLRs toll-like receptorsmedicine.symptomlcsh:Medicine (General)Oxidation-ReductionAP-1 activator protein-1Signal TransductionmRNA messenger ribonucleic acidHMGB1ASC apoptosis-associated speck-like protein containing a carboxy-terminal CARDRNS reactive nitrogen speciesPTPs protein tyrosine phosphatasesROS reactive oxygen speciesNADH nicotinamide adenine dinucleotidepHe extracellular pHFAEE fatty acid ethyl estersAP acute pancreatitisHumansXanthine oxidaseCBP CREB-binding proteinRyR endoplasmic reticulum membrane ryanodine receptorsMDA malondialdehydeNO nitric oxideXO xanthine oxidaseASK1 apoptosis signal-regulating kinase-1business.industryOrganic ChemistryAutophagyNADPH nicotinamide adenine dinucleotide phosphateHDACs histone deacetylasesmedicine.diseaseCARS compensatory anti-inflammatory response syndromeXDH xanthine dehydrogenaseIL interleukinIκB inhibitor of kappa BAcute pancreatitisETC Electron transport chainPancreatitisMKPs MAPK phosphatasesSAP severe acute pancreatitischemistrylcsh:Biology (General)DTT dithiothreitolOxidative stressNAC N-acetyl cysteineImmunologybiology.proteinCalciumLysosomesReactive Oxygen SpeciesbusinessMAPK mitogen-activated protein kinaseOxidative stressERCP endoscopic retrograde cholangiopancreatographyRedox Biology
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Antioxidant therapy counteracts the disturbing effects of diamide and maternal ageing on meiotic division and chromosomal segregation in mouse oocytes

1998

This study aims (i) to ascertain whether oxidative-stress-induced disturbances in chromosomal distribution in the metaphase-II spindle of mouse oocytes can be counteracted by supplementing culture medium with antioxidants; and (ii) to determine whether supplemental intake of antioxidants neutralizes the disturbing effects of maternal ageing on segregation of chromosomes during the first meiotic division and distribution of chromosomes in the metaphase-II spindle. (i): Germinal vesicle oocytes from unstimulated 10-12 week old mice were matured in vitro in the presence or absence of diamide and/or dithiothreitol. Metaphase-II oocytes were fixed and stained with 4',6-diamidino-2-phenylindole (…

OvulationAgingEmbryologymedicine.medical_treatmentAneuploidyAscorbic AcidBiologyAntioxidantsChromosomesAndrologyMiceMeiosisGeneticsmedicineAnimalsVitamin EMolecular BiologyMetaphaseMetaphaseDiamideGerminal vesicleVitamin EObstetrics and GynecologyKaryotypeCell BiologyAneuploidyOxidantsmedicine.diseaseOocyteAscorbic acidMice Inbred C57BLDithiothreitolMeiosisOxidative Stressmedicine.anatomical_structureReproductive MedicineBiochemistryDietary SupplementsMice Inbred CBAOocytesFemaleMaternal AgeDevelopmental BiologyMolecular Human Reproduction
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Redox regulation of enzymatic activity and proteolytic susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase fromEuglena gracilis.

1992

The activity of ribulose-1,5-bisphosphate carboxylase/oxygenase fromEuglena gracilis decays steadily when exposed to agents that induce oxidative modification of cysteine residues (Cu(2+), benzofuroxan, disulfides, arsenite, oxidized ascorbate). Inactivation takes place with a concomitant loss of cysteine sulfhydryl groups and dimerization of large subunits of the enzyme. 40% activity loss induced by the vicinal thiol-reagent arsenite is caused by modification of a few neighbor residues while the almost complete inactivation achieved with disulfides is due to extensive oxidation leading to formation of mixed disulfides with critical cysteines of the protein. In most cases oxidative inactiva…

OxygenaseCell BiologyPlant ScienceGeneral MedicineGlutathioneBiochemistryDithiothreitolPyruvate carboxylasechemistry.chemical_compoundchemistryBiochemistryCystamineCysteamineThioredoxinCysteinePhotosynthesis research
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Increased susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatments

1990

The susceptibility of the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolysis by trypsin, chymotrypsin, proteinase K, and papain is enhanced by oxidative treatments including spontaneous oxidation of cysteines. Proteinases exhibit a high specificity for the oxidized inactive form of the carboxylase, cleaving its large subunit. Treatment of the inactive enzyme with dithiothreitol results in partial recovery of both carboxylase activity and resistance to proteolysis. This behavior may explain the specific degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase that occurs in vivo during leaf senescence.

OxygenaseTime FactorsRibulose-Bisphosphate CarboxylaseProteolysisBiophysicsBiochemistryDithiothreitolchemistry.chemical_compoundEnzyme StabilitymedicineCysteineMolecular Biologychemistry.chemical_classificationChymotrypsinRibulose 15-bisphosphatebiologymedicine.diagnostic_testHydrolysisPlantsTrypsinPyruvate carboxylaseEnzymechemistryBiochemistrybiology.proteinOxidation-ReductionPeptide Hydrolasesmedicine.drugArchives of Biochemistry and Biophysics
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Analysis of serine proteases from marine sponges by 2-D zymography.

2007

Proteolytic activities isolated from the marine demosponges Geodia cydonium and Suberites domuncula were analyzed by 2-D zymography, a technique that combines IEF and zymography. After purification, a 200 kDa proteolytically active protein band was obtained from G. cydonium when analyzed in gelatin copolymerized 1-D zymograms. The enzymatic activity was quantified using alpha-N-benzoyl-D-arginine p-nitroanilide (BAPNA) as a substrate and corresponded to a serine protease. The protease activity was resistant to urea and SDS. DTT and 2-mercaptoethanol (2-ME) did not significantly change the protease activity, but induced a shift in molecular mass of the proteolytic band to lower M(r) values a…

Proteasesmedicine.medical_treatmentClinical BiochemistryBiologyBenzoylarginine NitroanilideBiochemistryAnalytical ChemistrySubstrate SpecificitySerinemedicineAnimalsUreaZymographyElectrophoresis Gel Two-DimensionalMercaptoethanolSerine proteasechemistry.chemical_classificationProteaseMolecular massSerine EndopeptidasesSodium Dodecyl Sulfatebiology.organism_classificationMolecular biologyPoriferaSuberites domunculaEnzyme ActivationMolecular WeightDithiothreitolEnzymeBiochemistrychemistrybiology.proteinElectrophoresis
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