{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,5]],"date-time":"2026-05-05T01:58:26Z","timestamp":1777946306084,"version":"3.51.4"},"reference-count":0,"publisher":"S. Karger AG","license":[{"start":{"date-parts":[[2009,4,24]],"date-time":"2009-04-24T00:00:00Z","timestamp":1240531200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/karger.com\/pages\/terms-and-conditions"},{"start":{"date-parts":[[2009,4,24]],"date-time":"2009-04-24T00:00:00Z","timestamp":1240531200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/karger.com\/pages\/terms-and-conditions"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Haemostasis"],"abstract":"<jats:p>Fibrolase, a fibrinolytic enzyme isolated from Agkistrodon c. contortrix (southern copperhead) venom, solubilizes fibrin primarily by rapid hydrolysis of the alpha and beta chains. Fibrolase is also an A\u03b1, B\u03b2 fibrinogenase. The breakdown products of fibrin and fibrinogen following incubation with fibrolase were different from those observed with plasmin. This enzyme is a metalloprotease that was inhibited by ethylenediaminetetraacetic acid. Fibrolase was inhibited by dithiothreitol, suggesting that disulfide bonds are important for catalytic activity. It was also inhibited by \u03b1&lt;sub&gt;2&lt;\/sub&gt;-macroglobulin, but not by the soybean or lima bean trypsin inhibitors, diisopropylfluorophosphate, or p-hydroxymercuribenzoate. Unlike thrombolytic agents such as streptokinase, fibrolase does not activate plasminogen as evidenced by the use of plasmin-specific chromogenic substrate S-2251 and by sodium do-decyl sulfate-polyacrylamide gel electrophoresis.<\/jats:p>","DOI":"10.1159\/000216121","type":"journal-article","created":{"date-parts":[[2009,4,24]],"date-time":"2009-04-24T09:41:27Z","timestamp":1240566087000},"page":"147-154","source":"Crossref","is-referenced-by-count":1,"title":["Biochemical Characteristics of Fibrolase, a Fibrinolytic Protease from Snake Venom"],"prefix":"10.1159","author":[{"given":"N.K.","family":"Ahmed","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K.D.","family":"Tennant","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F.S.","family":"Markland","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.P.","family":"Lacz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"127","published-online":{"date-parts":[[2009,4,24]]},"container-title":["Haemostasis"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.karger.com\/Article\/Pdf\/216121","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/karger.com\/article-pdf\/doi\/10.1159\/000216121","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,2]],"date-time":"2026-05-02T16:39:11Z","timestamp":1777739951000},"score":1,"resource":{"primary":{"URL":"https:\/\/karger.com\/article\/doi\/10.1159\/000216121"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,4,24]]},"references-count":0,"URL":"https:\/\/doi.org\/10.1159\/000216121","archive":["Portico"],"relation":{},"ISSN":["0301-0147","1423-0038"],"issn-type":[{"value":"0301-0147","type":"print"},{"value":"1423-0038","type":"electronic"}],"subject":[],"published":{"date-parts":[[2009,4,24]]}}}