Search results for "Nucleases"

showing 10 items of 147 documents

Different deoxyribonucleases in human lymphocytes

1974

Abstract The distribution pattern of deoxyribonuclease activities in human lymphocytes has been examined by micro-disc-electrophoresis. Four groups of deoxyribonuclease activities, differing in their electrophoretic mobility, in the nature of their optimal substrate and in their optimal incubation conditions, are characterized. There are two alkaline DNase-activities. One corresponds to DNase I (EC 3.1.4.5), the other having pH optimum of about pH 9.0, prefers denatured DNA as substrate and is not dependent on divalent cations. The fractions with an acid pH optimum can be subdivided into two groups, which differ in their activity towards native DNA, towards denatured DNA, in their activity …

Malechemistry.chemical_classificationDeoxyribonucleasesHot TemperatureSubstrate (chemistry)DeoxyribonucleaseHydrogen-Ion ConcentrationIn Vitro TechniquesBiologyDivalentElectrophoresischemistry.chemical_compoundchemistryBiochemistryGeneticsHumansElectrophoresis Polyacrylamide GelLymphocytesDeoxyribonuclease IDeoxyribonucleasesIncubationDNANucleic Acids Research
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Oxidative and lysosomal capacity in skeletal muscle of mice after endurance training of different intensities

1978

The activity of certain enzymes of energy metabolism (cytochrome c oxidase, citrate synthase, malate dehydrogenase, and lactate dehydrogenase) and of lysosomes (beta-glucuronidase, beta-N-acetylglucosamindase, arylsuphatase, ribonuclease, deoxyribonuclease, acid phosphatase, and cathepsin D) was assayed from m. rectus femoris of mice trained 5 days per week, 1 hr per day for 4 weeks according to 4 different programmes: I. running speed 20 m/min, horizontal track, II. 25 m/min, horizontal track, III. 20 m/min 8 degrees uphill inclination, and IV. 25 m/min 8 degrees uphill inclination. Oxidative capacity increased and anaerobic capacity decreased without distinction between the different tran…

Malemedicine.medical_specialtyPhysiologyAcid PhosphataseCathepsin DCitrate (si)-SynthaseMalate dehydrogenaseElectron Transport Complex IVMicechemistry.chemical_compoundRibonucleasesMalate DehydrogenaseEndurance trainingLactate dehydrogenaseInternal medicineAcetylglucosaminidasemedicineAnimalsCitrate synthaseCytochrome c oxidaseArylsulfatasesGlucuronidaseDeoxyribonucleasesPhysical Education and TrainingL-Lactate DehydrogenasebiologyHistocytochemistryMusclesAcid phosphataseSkeletal muscleCathepsinsEndocrinologymedicine.anatomical_structurechemistryBiochemistrybiology.proteinEnergy MetabolismLysosomesActa Physiologica Scandinavica
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Acid hydrolase activity in red and white skeletal muscle of mice during a two-week period following exhausting exercise

1978

The activities of beta-glucuronidase, beta-N-acetylglucosaminidase, arylsulphatase, ribonuclease, p-nitrophenylphosphatase, and malate dehydrogenase together with protein content were assayed from representative mixed (m. rectus femoris), predominantly red (proximal heads of m. vastus lateralis, m.v. medius and m. v. intermedius), and predominantly white (distal head of m. vastus lateralis) muscle homogenates of mice during a two-week period following one single exposure to exhausting intermittent running on a treadmill. The activities of cathepsin D and beta-glycerophosphatase were assayed from mixed muscle only. In all three muscle types, particularly in red muscle, the activities of beta…

Malemedicine.medical_specialtyTime FactorsHydrolasesPhysiologyAcid PhosphatasePhysical ExertionClinical BiochemistryPhosphataseCathepsin DBiologyMalate dehydrogenaseMiceRibonucleasesMalate DehydrogenasePhysiology (medical)Internal medicineAcetylglucosaminidasemedicineAnimalsTreadmillReceptorArylsulfatasesGlucuronidase4-NitrophenylphosphataseMusclesSkeletal musclebiology.organism_classificationCathepsinsMediusEndocrinologymedicine.anatomical_structurebiology.proteinAcid hydrolasePfl�gers Archiv European Journal of Physiology
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SYNTHESIS AND CHARACTERIZATION OF POLYAMINOACIDIC POLYCATIONS FOR GENE DELIVERY

2005

The properties as non viral gene vector of a protein-like polymer, the alpha,beta-poly(N-2-hydroxyethyl)-d,l-aspartamide (PHEA) were exploited after its derivatization with 3-(carboxypropyl)trimethyl-ammonium chloride (CPTA) as molecule bearing a cationic group, in order to obtain stable polycations able to condense DNA. PHEA was firstly functionalized with aminic pendant groups by reaction with ethylenediamine (EDA) obtaining the alpha,beta-poly(N-2-hydroxyethyl)(2-aminoethylcarbamate)-d,l-aspartamide (PHEA-EDA) copolymer. We demonstrated that polymer functionalization degree is easily modulable by varying reaction conditions, so allowing to produce two PHEA-EDA derivatives at different mo…

Materials scienceBiophysicsBioengineeringEthylenediamineGene deliveryPolycationBiomaterialschemistry.chemical_compoundGene DeliveryPolymer chemistryPolyaminesTumor Cells CulturedCopolymerHumansAspartameCytotoxicityEndodeoxyribonucleasesGene Transfer TechniquesCationic polymerizationDNACondensation reactionPolyelectrolytesPolyelectrolytechemistryMechanics of MaterialsCeramics and CompositesAmine gas treating
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FICC-Seq: a method for enzyme-specified profiling of methyl-5-uridine in cellular RNA.

2019

AbstractMethyl-5-uridine (m5U) is one the most abundant non-canonical bases present in cellular RNA, and in yeast is found at position U54 of tRNAs where modification is catalysed by the methyltransferase Trm2. Although the mammalian enzymes that catalyse m5U formation are yet to be identified via experimental evidence, based on sequence homology to Trm2, two candidates currently exist, TRMT2A and TRMT2B. Here we developed a genome-wide single-nucleotide resolution mapping method, Fluorouracil-Induced-Catalytic-Crosslinking-Sequencing (FICC-Seq), in order to identify the relevant enzymatic targets. We demonstrate that TRMT2A is responsible for the majority of m5U present in human RNA, and t…

MethyltransferaseSaccharomyces cerevisiae ProteinsCell SurvivalSaccharomyces cerevisiaeBiology03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferYeastsGeneticsHumansNucleotideUridine030304 developmental biologychemistry.chemical_classification0303 health sciencestRNA MethyltransferasesDeoxyribonucleasesHEK 293 cellsRNAHigh-Throughput Nucleotide SequencingYeastUridineEnzymeHEK293 CellsBiochemistrychemistry030220 oncology & carcinogenesisTransfer RNARNAMethods OnlineFluorouracilNucleic acids research
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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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Two copper complexes from two novel naphthalene-sulfonyl-triazole ligands: different nuclearity and different DNA binding and cleavage capabilities.

2013

[EN] Two novel naphthalene-sulfonyl-triazole ligands, 5-amino-N1-(naphthalen-3-ylsulfony1)-1,2,4-triazole (anstrz) and 3,5-diamino-N1-(naphthalen-3-ylsulfony1)-1,2,4-triazole (danstrz), purposely designed to interact with DNA, have been prepared for the first time and then fully characterized by H-1, C-13 NMR and IR spectroscopy, mass spectrometry and elemental analysis. The crystal structures of two copper complexes of these derivatives, i.e. [Cu(anstrz)(4)(NO3)(2)]center dot 4CH(3)OH (1), mononuclear, and [Cu(danstrz)(mu-OAc)(2)](2)center dot 2(danstrz) (OAc = acetato) (2), dinuclear, have been determined by single-crystal X-ray diffraction. In both cases the ligand coordinates in a monod…

Models MolecularDenticity124-Triazole ligandsStereochemistryTriazolePaddle wheel type copper acetate compoundCrystal structureNaphthalenesCrystallography X-RayLigandsBiochemistryInorganic Chemistrychemistry.chemical_compoundX-Ray DiffractionCoordination ComplexesBIOQUIMICA Y BIOLOGIA MOLECULARSulfonesBinding siteDNA CleavageCu(II)-triazole complexesBond cleavageNuclease activitySulfonylchemistry.chemical_classificationSulfonamidesBinding SitesDeoxyribonucleasesChemistryLigandDNATriazolesBinding constantDNA interactionCrystallographyCopperJournal of inorganic biochemistry
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Syntheses, crystal structures, and oxidative DNA cleavage of some Cu(II) complexes of 5-amino-3-pyridin-2-yl-1,2,4-triazole

2004

Three new monomeric Cu(II) complexes of 5-amino-3-pyridin-2-yl-1,2,4-triazole (Hapt), [Cu(Hapt)(H(2)O)(2)(SO(4))] (1), [Cu(Hapt)(2)(H(2)O)(NO(3))](NO(3)) (2), and [Cu(Hapt)(2)(NCS-N)](NCS).H(2)O (3), have been prepared and characterized by single crystal X-ray diffraction. One distorted [CuN(2)O(2)+O(')] square-pyramidal (1), one distorted [CuN(3)O+N(')+O(')] octahedral (2), and one distorted [CuN(4)+N(')] intermediate between square-pyramidal and trigonal-bipyramidal (3) coordination configuration were found and are suggested to be due to the chelating nature of the ligand, which interacts with Cu(II) through the N4(triazole) and N(pyridine) atoms. Spectral properties of these chelates are…

Models MolecularDeoxyribonucleasesMolecular StructureStereochemistryDimethyl sulfoxideLigandSpectrum AnalysisMolecular Sequence Data124-TriazoleDNAFree Radical ScavengersCrystal structureTriazolesCrystallography X-RayBiochemistryMedicinal chemistryInorganic Chemistrychemistry.chemical_compoundMonomerchemistryOctahedronSodium azideChelationOxidation-ReductionCopperJournal of Inorganic Biochemistry
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Copper-mediated DNA photocleavage by a tetrapyridoacridine (tpac) ligand.

2008

Abstract We have focused our interest on the tetrapyridoacridine ligand tetrapyrido[3,2- a :2′,3′- c :3′′,2″- h : 2‴,3‴- j ]acridine (tpac), as a model system for the preparation of novel copper-based artificial nucleases. The complex of copper(II)–tpac cleaves supercoiled pUC18 plasmid DNA in an oxidative manner by photoactivation with visible light, exhibiting maximum cleaving efficiency at 1:2 metal–ligand stoichiometric ratio. We propose an interaction of the copper–tpac complex with DNA through both major and minor grooves and a photocleavage mechanism via the formation of hydroxyl radicals and singlet oxygen or singlet oxygen-like species.

Models MolecularLightStereochemistryPhotochemistryRadicalClinical BiochemistryPharmaceutical Sciencechemistry.chemical_elementPhotochemistryLigandsBiochemistrychemistry.chemical_compoundPolycyclic compoundDrug DiscoveryPhotosensitizerSinglet stateMolecular Biologychemistry.chemical_classificationDeoxyribonucleasesMolecular StructureSinglet OxygenChemistrySinglet oxygenOrganic ChemistryDNACopperAcridineMolecular MedicineAcridinesDNACopperPhenanthrolinesBioorganicmedicinal chemistry letters
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AIF-1 and RNASET2 are involved in the inflammatory response in the Mediterranean mussel Mytilus galloprovincialis following Vibrio infection

2022

Filter-feeding bivalves, such as the Mytilus species, are exposed to different types of bacteria in the surrounding waters, in particular of the Vibrio genus. Mussels lack an adaptive immune system and hemocytes can recognize pathogen-associated molecular patterns (PAMPs) via pattern recognition receptors (PRRs) to activate intracellular signaling pathways to trigger the antimicrobial effectors synthesis. Among the areas of bivalve immunity that deserve study include the role of hemocyte subpopulations. Since little information are available on immune responses at the tissue level to human pathogenic vibrios commonly detected in coastal waters involved in seafood-borne diseases, in this wor…

MytilusHemocytesTumor Suppressor ProteinsAIF-1 Bacterial challenge Cellular immunity Immunohistochemistrym M. galloprovincialis Myd88 RNASET2 TLR4RNASET2General MedicineAquatic ScienceAIF-1; Bacterial challenge; Cellular immunity; Immunohistochemistry; M. galloprovincialis; Myd88; RNASET2; TLR4Myd88ImmunohistochemistryCellular immunityToll-Like Receptor 4Bacterial challengeRibonucleasesSeafoodVibrio InfectionsMyeloid Differentiation Factor 88Environmental ChemistryAnimalsHumansTLR4M. galloprovincialisAIF-1Vibrio
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