Toxicon : official journal of the International Society on Toxinology · 2007
Identification and characterization of a new member of snake venom thrombin inhibitors from Bothrops insularis using a proteomic approach.
СтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод в очереди
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Oliveira-Carvalho Ana Lúcia, Guimarães Patrícia Ramos, Abreu Paula Alvarez, Dutra Denis L S, Junqueira-de-Azevedo Inácio L M, Rodrigues Carlos Rangel, Ho Paulo Lee, Castro Helena C, Zingali Russolina B
Аннотация
Snake venom C-type lectin-like proteins (CLPs) are ubiquitously found in Viperidae snake venoms and differ from the C-type lectins as they display different biological activities but no carbohydrate-binding activity. Previous analysis of the transcriptome obtained from the Bothrops insularis venom gland showed the presence of two clusters homologous to bothrojaracin (BJC) chains alpha and beta. In an effort to identify a new BJC-like molecule, we used an approach associated with proteomic technologies to identify the presence of the expressed protein and then to purify and characterize a new thrombin inhibitor from B. insularis venom. We also constructed homology models of this protein and BJC, which were compared with other C-type lectin-like family members and revealed several conserved features of this intriguing snake venom toxin family.