Purification and Characterization of BmooAi: A New Toxin from Bothrops moojeni Snake Venom That Inhibits Platelet Aggregation

dc.creatorQueiroz, Mayara Ribeiro de
dc.creatorMamede, Carla Cristine N.
dc.creatorMorais, Nadia Cristina G. de
dc.creatorFonseca, Kelly Cortes
dc.creatorSousa, Bruna Barbosa de
dc.creatorMigliorini, Thaís M.
dc.creatorPereira, Déborah Fernanda C.
dc.creatorStanziola, Leonilda
dc.creatorCalderon, Leonardo A.
dc.creatorSilva, Rodrigo Simões
dc.creatorSoares, Andreimar Martins
dc.creatorOliveira, Fábio de
dc.date2016-04-19T13:40:24Z
dc.date2016-04-19T13:40:24Z
dc.date2014
dc.date.accessioned2023-09-26T20:13:32Z
dc.date.available2023-09-26T20:13:32Z
dc.identifierCALDERON, L. A. et al. Purification and Characterization of BmooAi: A New Toxin from Bothrops moojeni Snake Venom That Inhibits Platelet Aggregation. BioMed Research International, v. 2014, p. 1-7, 2014.
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/13861
dc.identifierhttp://dx.doi.org/10.1155/2014/920942
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8851835
dc.descriptionIn this paper, we describe the purification/characterization of BmooAi, a new toxin from Bothrops moojeni that inhibits platelet aggregation. The purification of BmooAi was carried out through three chromatographic steps (ion-exchange on a DEAE-Sephacel column, molecular exclusion on a Sephadex G-75 column, and reverse-phase HPLC chromatography on a C2/C18 column). BmooAi was homogeneous by SDS-PAGE and shown to be a single-chain protein of 15,000 Da. BmooAi was analysed by MALDI-TOF Spectrometry and revealed two major components with molecular masses 7824.4 and 7409.2 as well as a trace of protein with a molecular mass of 15,237.4 Da. Sequencing of BmooAi by Edman degradation showed two amino acid sequences: IRDFDPLTNAPENTA and ETEEGAEEGTQ, which revealed no homology to any known toxin from snake venom. BmooAi showed a rather specific inhibitory effect on platelet aggregation induced by collagen, adenosine diphosphate, or epinephrine in human platelet-rich plasma in a dose-dependent manner, whereas it had little or no effect on platelet aggregation induced by ristocetin. The effect on platelet aggregation induced by BmooAi remained active even when heated to 100∘C. BmooAi could be of medical interest as a new tool for the development of novel therapeutic agents for the prevention and treatment of thrombotic disorders.
dc.formatapplication/pdf
dc.languageeng
dc.publisherBioMed Research International
dc.rightsopen access
dc.subjectBmooAi
dc.subjectNew Toxin
dc.subjectBothrops moojeni
dc.subjectSnake Venom
dc.subjectPlatelet Aggregation
dc.titlePurification and Characterization of BmooAi: A New Toxin from Bothrops moojeni Snake Venom That Inhibits Platelet Aggregation
dc.typeArticle


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