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dc.typeArtigo de periódicopt_BR
dc.titleNeuromuscular Activity Of Batx, A Presynaptic Basic Pla2 Isolated From Bothrops Alternatus Snake Venom.pt_BR
dc.contributor.authorPonce-Soto, L Apt_BR
dc.contributor.authorBarros, J Cpt_BR
dc.contributor.authorMarangoni, Spt_BR
dc.contributor.authorHernandez, Spt_BR
dc.contributor.authorDal Belo, C Apt_BR
dc.contributor.authorCorrado, A Ppt_BR
dc.contributor.authorHyslop, Spt_BR
dc.contributor.authorRodrigues-Simioni, Lpt_BR
unicamp.authorL A Ponce-Soto, Departamento de Farmacologia, Faculdade de Ciências Médicas, Universidade Estadual de Campinas , CP 6111, Campinas, SP, Brazil.pt_BR C Barros,pt Marangoni,pt Hernandez,pt A Dal Belo,pt P Corrado,pt Hyslop,pt Rodrigues-Simioni,pt
dc.subjectChick Embryopt_BR
dc.subjectCholinergic Agonistspt_BR
dc.subjectChromatography, High Pressure Liquidpt_BR
dc.subjectCrotalid Venomspt_BR
dc.subjectDose-response Relationship, Drugpt_BR
dc.subjectElectric Stimulationpt_BR
dc.subjectElectrophoresis, Polyacrylamide Gelpt_BR
dc.subjectMiniature Postsynaptic Potentialspt_BR
dc.subjectMolecular Weightpt_BR
dc.subjectNeuromuscular Blocking Agentspt_BR
dc.subjectNeuromuscular Junctionpt_BR
dc.subjectPhospholipases A2pt_BR
dc.subjectPhrenic Nervept_BR
dc.subjectPresynaptic Terminalspt_BR
dc.subjectSequence Analysis, Proteinpt_BR
dc.subjectSpectrometry, Mass, Matrix-assisted Laser Desorption-ionizationpt_BR
dc.subjectSynaptic Transmissionpt_BR
dc.subjectTime Factorspt_BR
dc.description.abstractWe have previously isolated a Lys49 phospholipase A(2) homolog (BaTX) from Bothrops alternatus snake venom using a combination of molecular exclusion chromatography and reverse phase HPLC and shown its ability to cause neuromuscular blockade. In this work, we describe a one-step procedure for the purification of this toxin and provide further details of its neuromuscular activity. The toxin was purified by reverse phase HPLC and its purity and molecular mass were confirmed by SDS-PAGE, MALDI-TOF mass spectrometry, amino acid analysis and N-terminal sequencing. BaTX (0.007-1.4 microM) produced time-dependent, irreversible neuromuscular blockade in isolated mouse phrenic nerve-diaphragm and chick biventer cervicis preparations (time to 50% blockade with 0.35 microM toxin: 58+/-4 and 24+/-1 min, respectively; n=3-8; mean+/-S.E.) without significantly affecting the response to direct muscle stimulation. In chick preparations, contractures to exogenous acetylcholine (55 and 110 microM) or KCl (13.4 mM) were unaltered after complete blockade by all toxin concentrations. These results, which strongly suggested a presynaptic mechanism of action for this toxin, were reinforced by (1) the inability of BaTX to interfere with the carbachol-induced depolarization of the resting membrane, (2) a significant decrease in the frequency and amplitude of miniature end-plate potentials, and (3) a significant reduction (59+/-4%, n=12) in the quantal content of the end-plate potentials after a 60 min incubation with the toxin (1.4 microM). In addition, a decrease in the organ bath temperature from 37 degrees C to 24 degrees C and/or the replacement of calcium with strontium prevented the neuromuscular blockade, indicating a temperature-dependent effect possibly mediated by enzymatic activity.en
dc.relation.ispartofComparative Biochemistry And Physiology. Toxicology & Pharmacology : Cbppt_BR
dc.relation.ispartofabbreviationComp. Biochem. Physiol. C Toxicol. Pharmacol.pt_BR
dc.identifier.citationComparative Biochemistry And Physiology. Toxicology & Pharmacology : Cbp. v. 150, n. 2, p. 291-7, 2009-Aug.pt_BR
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