Search results for "Dinucleoside Phosphates"

showing 3 items of 3 documents

Pre- and postjunctional effects of diadenosine polyphosphates in the guinea-pig vas deferens.

1995

Abstract The pre- and postjunctional activities of a number of diadenosine polyphosphates were examined in the guinea-pig isolated vas deferens at the level of the membrane-potential, using a modified sucrose-gap technique. P1,P3-Di(adenosine 5′)triphosphate (Ap3A), P1,P4-di(adenosine 5′)tetraphosphate (Ap4A) and P1,P5-di(adenosine 5′)pentaphosphate (Ap5 A) all caused concentration-dependent depolarization of the smooth muscle membrane. The potency order was: Ap5A > Ap4A. Ap3A. P1, P2-Di(adenosine 5′)pyrophosphate (Ap2A) did not evoke depolarization even at the highest concentration tested (1 mM). All the dinucleotides caused a reduction in the amplitude of evoked excitatory junction…

Malemedicine.medical_specialtyGuinea PigsPharmaceutical ScienceIn Vitro TechniquesMembrane PotentialsVas DeferensAdenine nucleotideInternal medicinemedicineAnimalsPharmacologyDose-Response Relationship DrugChemistryPurinergic receptorAntagonistVas deferensReceptors PurinergicDepolarizationAdenosine receptorAdenosinemedicine.anatomical_structureEndocrinologyExcitatory postsynaptic potentialDinucleoside Phosphatesmedicine.drugThe Journal of pharmacy and pharmacology
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Poly(U) RNA-templated synthesis of AppA.

2015

Simple nucleotide templating activities are of interest as potential primordial reactions. Here we describe the acceleration of 5′-5′ AppA synthesis by 3′-5′ poly(U) under normal solution conditions. This reaction is apparently templated via complementary U:A base-pairing, despite the involvement of two different RNA backbones, because poly(U), unlike other polymers, significantly stimulates AppA synthesis. These interactions occur in moderate (K+) and (Mg2+) and are temperature sensitive, being more efficient at 10°C than at 4°C, but absent at 20°C. The reaction is only slightly pH sensitive, despite potentially relevant substrate pKa’s. Kinetic data explicitly support production of AppA b…

chemistry.chemical_classificationPoly UbiologyMolecular modelStereochemistryRNASubstrate (chemistry)Chemical reactionCofactorArticlechemistryBiochemistrybiology.proteinMoleculeRNANucleotideMolecular BiologyDinucleoside PhosphatesDinucleoside PhosphatesRNA (New York, N.Y.)
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Muscle adenylate kinase in Duchenne muscular dystrophy

1986

Abstract On the basis of electrophoretic and enzyme inhibition studies it was postulated that an aberrant adenylate kinase occurs in muscle and serum of patients with Duchenne muscular dystrophy (Schirmer, R.H. and Thuma, E. (1972) Biochim. Biophys. Acta 268, 92–97; Hamada, M. et al. (1981) Biochim. Biophys. Acta 660, 227–237; Hamada et al. (1985) J. Biol. Chem. 260, 11595–11602. On the basis of the following results we conclude that Duchenne muscular dystrophy patients do not possess an unusual adenylate kinase isoenzyme. (1) In muscle biopsies from five Duchenne patients, the electrophoretic mobility of adenylate kinase and the inhibition of the enzyme by P 1 , P 5 -di(adenosine-5′)pentap…

medicine.medical_specialtyDTNBDuchenne muscular dystrophyBiophysicsAdenylate kinaseDithionitrobenzoic AcidBiochemistryIsozymeMuscular Dystrophieschemistry.chemical_compoundNormal muscleInternal medicinemedicineHumansheterocyclic compoundsSulfhydryl CompoundsMolecular Biologychemistry.chemical_classificationAdenine NucleotidesMusclesAdenylate KinasePhosphotransferasesElectrophoresis Cellulose Acetatemedicine.diseaseMOPSIsoenzymesEndocrinologyEnzymechemistryPMSFDinucleoside PhosphatesBiochimica et Biophysica Acta (BBA) - General Subjects
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