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Two novel proteins, jararhagin and jaracetin, were purified from Bothrops jararaca viper venom. Jararhagin is a 55-kDa member of the metalloprotease-disintegrin family. Jaracetin is a 60-kDa dimer representing a differently processed form of jararhagin. Like botrocetin, a previously described viper venom protein, jararhagin and jaracetin modulated binding of von Willebrand Factor to the glycoprotein Ib-IX complex on platelets through a specific interaction with the von Willebrand Factor A1 domain. Both jararhagin and jaracetin, but not botrocetin, also blocked alpha 2 beta 1-dependent platelet adhesion to collagen, a receptor interaction mediated through a homologous A domain on the integrin alpha 2 subunit.


M De Luca, C M Ward, K Ohmori, R K Andrews, M C Berndt. Jararhagin and jaracetin: novel snake venom inhibitors of the integrin collagen receptor, alpha 2 beta 1. Biochemical and biophysical research communications. 1995 Jan 17;206(2):570-6

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PMID: 7530003

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