Navegando por Palavras-chave "heparin affinity"

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    Cloning, Characterization and Anti-Inflammatory Properties of Bothrops jararaca Snake Antithrombin
    (Bentham Science Publ Ltd, 2015-01-01) Morais-Zani, Karen de; Grego, Kathleen Fernandes; Torquato, Ricardo José Soares [UNIFESP]; Silva, Caroline Serino; Tanaka, Aparecida Sadae [UNIFESP]; Tanaka-Azevedo, Anita Mitico; Inst Butantan; Universidade de São Paulo (USP); Universidade Federal de São Paulo (UNIFESP)
    Antithrombin inhibits blood coagulation through the interaction with serine proteases in both intrinsic and extrinsic pathways. In addition, antithrombin also shows anti-inflammatory properties, which are independent of its effects on coagulation. This work shows for the first time the cloning and sequencing of antithrombin from a snake species. This predicted protein is composed by 430 amino acids and presents about 64.5% sequence identity to human antithrombin. Biacore experiments revealed that the binding affinity of Bothrops jararaca snake antithrombin to heparin was similar to 30 times higher than that of human antithrombin. Furthermore, Bothrops jararaca antithrombin is more effective in preventing acute inflammation induced by carrageenan when compared to human antithrombin. Hence, the results showed herein suggest that Bothrops jararaca antithrombin can play a key role in the control of acute inflammation and that this molecule might be used as a pharmacological tool and as a prototype for drug development.