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The toxin was purified by a combination of three chromatographic steps (ion-exchange on DEAE-Sephacel, molecular exclusion on Sephadex G-75, and affinity chromatography on HiTrap\u2122 Heparin HP). BmooPAi was found to be a single-chain protein with an apparent molecular mass of 32\u2009kDa on 14% SDS-PAGE, under reducing conditions. Sequencing of BmooPAi by Edman degradation revealed the amino acid sequence LGPDIVPPNELLEVM. The toxin was devoid of proteolytic, haemorrhagic, defibrinating, or coagulant activities and induced no significant oedema or hyperalgesia. BmooPAi showed a rather specific inhibitory effect on ristocetin-induced platelet aggregation in human platelet-rich plasma, whereas it had little or no effect on platelet aggregation induced by collagen and adenosine diphosphate. The results presented in this work suggest that BmooPAi is a toxin comprised of disintegrin-like and cysteine-rich domains, originating from autolysis\/proteolysis of PIII SVMPs from<jats:italic>B. moojeni<\/jats:italic>snake venom. This toxin may be of medical interest because it is a platelet aggregation inhibitor, which could potentially be developed as a novel therapeutic agent to prevent and\/or treat patients with thrombotic disorders.<\/jats:p>","DOI":"10.1155\/2017\/4315832","type":"journal-article","created":{"date-parts":[[2017,11,1]],"date-time":"2017-11-01T23:31:24Z","timestamp":1509579084000},"page":"1-9","source":"Crossref","is-referenced-by-count":5,"title":["A New Platelet-Aggregation-Inhibiting Factor Isolated from<i>Bothrops moojeni<\/i>Snake Venom"],"prefix":"10.1155","volume":"2017","author":[{"given":"Bruna Barbosa de","family":"Sousa","sequence":"first","affiliation":[{"name":"Instituto de Gen\u00e9tica e Bioqu\u00edmica, Universidade Federal de Uberl\u00e2ndia, Uberl\u00e2ndia, MG, Brazil"},{"name":"Instituto Nacional de Ci\u00eancia e Tecnologia em Nano-Biofarmac\u00eautica (N-Biofar), Belo Horizonte, MG, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carla Cristine 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