{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T21:15:43Z","timestamp":1760044543356},"reference-count":34,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2004,7,16]],"date-time":"2004-07-16T00:00:00Z","timestamp":1089936000000},"content-version":"vor","delay-in-days":2510,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1997,9]]},"abstract":"<jats:p>Bothrojaracin is a potent and selective thrombin inhibitor that has been isolated from the venom of <jats:italic>Bothrops jararaca.<\/jats:italic> It does not interact with the catalytic site of the enzyme but binds to both anion\u2010binding exosites 1 and 2 resulting in a potent inhibition of thrombin activity towards fibrinogen and platelets [<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"#b15\">Zingali, R. B., Jandrot\u2010Perrus, M., Guillin, M. C. &amp; Bon, C. (1993)<\/jats:ext-link><jats:italic>Biochemistry 32<\/jats:italic>, 10794\u201310802]. Bothrojaracin is a 27\u2010kDa protein composed of two disulfide\u2010linked polypeptide chains, A and B, of 15 kDa and 13 kDa, respectively. The sequences of A and B chains determined by molecular cloning exhibit a high degree of identity with other snake venom lectin\u2010like proteins. In contrast to other ligands that interact with thrombin exosite 1, the amino acid sequence of bothrojaracin does not contain an acidic sequence similar to the C\u2010terminal tail of hirudin. Expression of functional bothrojaracin was achieved in COS cells upon transfection with two pcDNA3 vectors containing the complete cDNAs. Recombinant bothrojaracin, which was secreted into the medium, was able to bind to and inhibit thrombin. When expressed alone, the B chain formed inactive dimers that were secreted into the culture medium. 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