{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:31:34Z","timestamp":1792787494543,"version":"4.5.0"},"reference-count":52,"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\/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"}]},{"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"}]},{"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>\n                    The present study aimed to evaluate the proteolytic and biological activities of a new metalloproteinase from\n                    <jats:italic>B. moojeni<\/jats:italic>\n                    venom. The purification of BmooMP\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -II was carried out through two chromatographic steps (ion-exchange and affinity). BmooMP\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -II is a monomeric protein with an apparent molecular mass of 22.5\u2009kDa on SDS-PAGE 14% under nonreducing conditions. The N-terminal sequence (FSPRYIELVVVADHGMFTKYKSNLN) revealed homology with other snake venom metalloproteinases, mainly among P-I class. BmooMP\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -II cleaves A\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -chain of fibrinogen followed by B\n                    <jats:italic>\u03b2<\/jats:italic>\n                    -chain, and does not show any effect on the\n                    <jats:italic>\u03b3<\/jats:italic>\n                    -chain. Its optimum temperature and pH for the fibrinogenolytic activity were 30\u201350\u00b0C and pH 8, respectively. The inhibitory effects of EDTA and 1,10-phenantroline on the fibrinogenolytic activity suggest that BmooMP\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -II is a metalloproteinase. This proteinase was devoid of haemorrhagic, coagulant, or anticoagulant activities. BmooMP\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -II caused morphological alterations in liver, lung, kidney, and muscle of Swiss mice. The enzymatically active protein yet inhibited collagen, ADP, and ristocetin-induced platelet aggregation in a concentration-dependent manner. Our results suggest that BmooMP\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -II contributes to the toxic effect of the envenomation and that more investigations to elucidate the mechanisms of inhibition of platelet aggregation may contribute to the studies of snake venom on thrombotic disorders.\n                  <\/jats:p>","DOI":"10.1155\/2014\/352420","type":"journal-article","created":{"date-parts":[[2014,6,1]],"date-time":"2014-06-01T17:05:23Z","timestamp":1401642323000},"page":"1-12","source":"Crossref","is-referenced-by-count":13,"title":["Rapid Purification of a New P-I Class Metalloproteinase from\n                    <i>Bothrops moojeni<\/i>\n                    Venom with Antiplatelet Activity"],"prefix":"10.1155","volume":"2014","author":[{"given":"Mayara R.","family":"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":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carla C. 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G.","family":"de Morais","sequence":"additional","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":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruna B.","family":"de Sousa","sequence":"additional","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":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norival A.","family":"Santos-Filho","sequence":"additional","affiliation":[{"name":"Faculdade de Ci\u00eancias Farmac\u00eauticas de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo, 14040-903 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