{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T20:29:06Z","timestamp":1740169746539,"version":"3.37.3"},"reference-count":37,"publisher":"Wiley","license":[{"start":{"date-parts":[[2014,1,1]],"date-time":"2014-01-01T00:00:00Z","timestamp":1388534400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"funder":[{"DOI":"10.13039\/501100004901","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de Minas Gerais","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004901","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Minist\u00e9rio de Ci\u00eancias e Tecnologia"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["BioMed Research International"],"published-print":{"date-parts":[[2014]]},"abstract":"<jats:p>In this paper, we describe the purification\/characterization of BmooAi, a new toxin from<jats:italic>Bothrops moojeni<\/jats:italic>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\u00b0C. 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.<\/jats:p>","DOI":"10.1155\/2014\/920942","type":"journal-article","created":{"date-parts":[[2014,5,29]],"date-time":"2014-05-29T17:14:26Z","timestamp":1401383666000},"page":"1-7","source":"Crossref","is-referenced-by-count":2,"title":["Purification and Characterization of BmooAi: A New Toxin from<i>Bothrops moojeni<\/i>Snake Venom That Inhibits Platelet Aggregation"],"prefix":"10.1155","volume":"2014","author":[{"given":"Mayara","family":"Ribeiro de Queiroz","sequence":"first","affiliation":[{"name":"Instituto de Gen\u00e9tica e Bioqu\u00edmica, Universidade Federal de Uberl\u00e2ndia, 38400-902 Uberl\u00e2ndia, MG, Brazil"},{"name":"Instituto Nacional de Ci\u00eancia e Tecnologia em Nano-Biofarmac\u00eautica (N-Biofar), 31270-901 Belo Horizonte, MG, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carla 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