Neuromuscular action of Bothrops lanceolatus (Fer de lance) venom and a caseinolytic fraction

dc.creatorde Araujo, AL
dc.creatorDonato, JL
dc.creatorLeite, GB
dc.creatorPrado-Franceschi, J
dc.creatorFontana, MD
dc.creatorBon, C
dc.creatorSimioni, LR
dc.date2002
dc.dateSEP
dc.date2014-11-18T11:50:57Z
dc.date2015-11-26T16:54:34Z
dc.date2014-11-18T11:50:57Z
dc.date2015-11-26T16:54:34Z
dc.date.accessioned2018-03-28T23:41:51Z
dc.date.available2018-03-28T23:41:51Z
dc.identifierToxicon. Pergamon-elsevier Science Ltd, v. 40, n. 9, n. 1283, n. 1289, 2002.
dc.identifier0041-0101
dc.identifierWOS:000178603500005
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/65289
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/65289
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/65289
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1276891
dc.descriptionA protein capable of inducing neuromuscular blockade in avian preparations and of depolarizing mouse diaphragm muscle was isolated from Bothrops lanceolatus venom using gel filtration and ion-exchange chromatography. The purified protein was a single chain polypeptide with an estimated molecular mass of 27.5 kDa by SDS-PAGE and had caseinolytic activity (13.3 units/mg), but no phospholipase A(2). B. lanceolatus venom (50 mug/ml) and the caseinolytic protein (20 mug/ml) produced contracture and progressive irreversible blockade (50% in 25 +/- 5 min (SEM) and 45 +/- 15 min, respectively), in indirectly stimulated chick biventer cervicis preparations. The contractile responses to acetylcholine (ACh; 37 and 74 muM, n = 6) were inhibited by venom and the caseinolytic protein, whereas those to potassium (13.4 mM, n = 6) were not. Membrane resting potential measurements in mouse hemidiaphragm preparations showed that B. lanceolatus venom and the purified protein caused depolarization which was prevented by D-tubocurarine (14.6 mM). The venom produced a slight increase in the amplitude and frequency of miniature end-plate potentials, but this effect was not seen with the purified fraction. These results suggest that the purified protein acts exclusively post-synaptically. (C) 2002 Published by Elsevier Science Ltd.
dc.description40
dc.description9
dc.description1283
dc.description1289
dc.languageen
dc.publisherPergamon-elsevier Science Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationToxicon
dc.relationToxicon
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectneuromuscular blockade
dc.subjectBothrops lanceolatus
dc.subjectpurified protein
dc.subjectNerve-muscle Preparation
dc.subjectPurification
dc.subjectEnzyme
dc.subjectMouse
dc.titleNeuromuscular action of Bothrops lanceolatus (Fer de lance) venom and a caseinolytic fraction
dc.typeArtículos de revistas


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