Navegando por Palavras-chave "Bothrops jararaca snake"

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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.
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    Isolation and identification of angiotensin-like peptides from the plasma of the snake Bothrops jararaca
    (Elsevier B.V., 1996-03-01) Borgheresi, RAMB; DalleLucca, J.; Carmona, E.; Picarelli, Z. P.; Universidade Federal de São Paulo (UNIFESP)
    Two distinct hypertensive peptides were purified and characterized from Bothrops jararaca (Bj) plasma incubated at pH 4, 37 degrees C, 24 hr. These peptides were active on rat and Bj blood pressure, on rat isolated uterus, on guinea-pig isolated ileum and on Bj isolated duodenum. At the releasing conditions no further activities were found for kininases, angiotensinases or angiotensin converting enzymes. the peptides were purified by ethanol/ether extraction, Sephadex G-25 gel filtration, semipreparative reverse-phase (C-18) HPLC and analytical (C-18) HPLC. the amino-acid sequences of the purified peptides corresponded to (Ile(5))AII and (Val(5)-Tyr(9))AI and their molecular masses were confirmed by mass spectrometry as 1046.6 and 1348.0 respectively. the presence oi those two angiotensins on Bj plasma may have some evolutionary significance since (Ile(5))AII is known as a mammalian angiotensin and (Val(5))AII as a non-mammalian one.