{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T20:46:09Z","timestamp":1790628369072,"version":"4.1.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2003,1,1]]},"abstract":"<jats:p>A novel prothrombin activator enzyme, which we have named \u2018berythractivase\u2019, was isolated from Bothrops erythromelas (jararaca-da-seca) snake venom. Berythractivase was purified by a single cation-exchange-chromatography step on a Resource S (Amersham Biosciences) column. The overall purification (31-fold) indicates that berythractivase comprises about 5% of the crude venom. It is a single-chain protein with a molecular mass of 78kDa. SDS\/PAGE of prothrombin after activation by berythractivase showed fragment patterns similar to those generated by group A prothrombin activators, which convert prothrombin into meizothrombin, independent of the prothrombinase complex. Chelating agents, such as EDTA and o-phenanthroline, rapidly inhibited the enzymic activity of berythractivase, like a typical metalloproteinase. Human fibrinogen A\u03b1-chain was slowly digested only after longer incubation with berythractivase, and no effect on the \u03b2- or \u03b3-chains was observed. Berythractivase was also capable of triggering endothelial proinflammatory and procoagulant cell responses. von Willebrand factor was released, and the surface expression of both intracellular adhesion molecule-1 and E-selectin was up-regulated by berythractivase in cultured human umbilical-vein endothelial cells. The complete berythractivase cDNA was cloned from a B. erythromelas venom-gland cDNA library. The cDNA sequence possesses 2330bp and encodes a preproprotein with significant sequence similarity to many other mature metalloproteinases reported from snake venoms. Berythractivase contains metalloproteinase, desintegrin-like and cysteine-rich domains. However, berythractivase did not elicit any haemorrhagic response. These results show that, although the primary structure of berythractivase is related to that of snake-venom haemorrhagic metalloproteinases and functionally similar to group A prothrombin activators, it is a prothrombin activator devoid of haemorrhagic activity. This is a feature not observed for most of the snake venom metalloproteinases, including the group A prothrombin activators.<\/jats:p>","DOI":"10.1042\/bj20020449","type":"journal-article","created":{"date-parts":[[2002,12,16]],"date-time":"2002-12-16T12:31:56Z","timestamp":1040041916000},"page":"129-139","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":84,"title":["A prothrombin activator from Bothrops erythromelas (jararaca-da-seca) snake venom: characterization and molecular cloning"],"prefix":"10.1042","volume":"369","author":[{"given":"M\u00e1rcia B.","family":"SILVA","sequence":"first","affiliation":[{"name":"Departamento do Biof\u00edsica, Universidade Federal de Pernambuco, Recife, PE, Brazil"},{"name":"Laborat\u00f3rio do Bioqu\u00edmica e Biof\u00edsica, Instituto Butantan, Av. Vital Brazil, 1500 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mirta","family":"SCHATTNER","sequence":"additional","affiliation":[{"name":"Departamento de Trombosis y Hemostasia, Academia Nacional de Medicina, Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas (CONICET), Buenos Aires, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Celso R.R.","family":"RAMOS","sequence":"additional","affiliation":[{"name":"Centro Do Biotecnolgia, Instituto Butantan, Av. Vital Brazil, 1500 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"In\u00e1cio L.M.","family":"JUNQUEIRA-de-AZEVEDO","sequence":"additional","affiliation":[{"name":"Centro Do Biotecnolgia, Instituto Butantan, Av. Vital Brazil, 1500 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M\u00edriam C.","family":"GUARNIERI","sequence":"additional","affiliation":[{"name":"Departamento do Zoologia, Universidade Federal de Pernambuco, Recife, PE, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mar\u00eda A.","family":"LAZZARI","sequence":"additional","affiliation":[{"name":"Departamento de Trombosis y Hemostasia, Academia Nacional de Medicina, Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas (CONICET), Buenos Aires, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudio A.M.","family":"SAMPAIO","sequence":"additional","affiliation":[{"name":"Departamento do Bioqu\u00edmica, Universidade Federal de S\u00e3o Paulo-Escola Paulista de Medicina (UNIFESP-EPM), SP, Brazil,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberto G.","family":"POZNER","sequence":"additional","affiliation":[{"name":"Departamento de Trombosis y Hemostasia, Academia Nacional de Medicina, Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas (CONICET), Buenos Aires, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janaina S.","family":"VENTURA","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio do Bioqu\u00edmica e Biof\u00edsica, Instituto Butantan, Av. Vital Brazil, 1500 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paulo L.","family":"HO","sequence":"additional","affiliation":[{"name":"Centro Do Biotecnolgia, Instituto Butantan, Av. Vital Brazil, 1500 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana M.","family":"CHUDZINSKI-TAVASSI","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio do Bioqu\u00edmica e Biof\u00edsica, Instituto Butantan, Av. Vital Brazil, 1500 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/369\/1\/129\/709447\/bj3690129.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/369\/1\/129\/709447\/bj3690129.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T11:56:54Z","timestamp":1637582214000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/369\/1\/129\/39785\/A-prothrombin-activator-from-Bothrops-erythromelas"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,1,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2003,1,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20020449","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2003,1,1]]}}}