Biochemical and functional properties of a thrombin-like enzyme isolated from Bothrops pauloensis snake venom
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Data
2009-11-01
Autores
Costa, Fabio L. S.
Rodrigues, Renata S.
Izidoro, Luiz F. M.
Menaldo, Danilo L.
Hamaguchi, Amelia
Homsi-Brandeburgo, Maria I.
Fuly, Andre L.
Soares, Sandro G.
Selistre-de-Araujo, Heloisa S.
Barraviera, Benedito [UNESP]
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Editor
Pergamon-Elsevier B.V. Ltd
Resumo
In the present study, a thrombin-like enzyme named BpSP-I was isolated from Bothrops pauloensis snake venom and its biochemical, enzymatic and pharmacological characteristics were determined. BpSP-I is a glycoprotein that contains both N-linked carbohydrates and sialic acid in its structure, with M(r) = 34,000 under reducing conditions and pI similar to 6.4. The N-terminal sequence of the enzyme (VIGGDECDINEHPFL) showed high similarity with other thrombin-like enzymes from snake venoms. BpSP-I showed high clotting activity upon bovine and human plasma and was inhibited by PMSF, benzamidine and leupeptin. Moreover, this enzyme showed stability when examined at different temperatures (-70 to 37 degrees C), pH values (3-9) or in the presence of divalent metal ions (Ca(2+), Mg(2+), Zn(2+) and Mn(2+)). BpSP-I showed high catalytic activity upon substrates, such as fibrinogen, TAME, S-2238 and S-2288. It also showed kallikrein-like activity, but was unable to act upon factor Xa and plasmin substrates. Indeed, the enzyme did not induce hemorrhage, myotoxicity or edema. Taken together, our data showed that BpSP-I is in fact a thrombin-like enzyme isoform isolated from Bothrops pauloensis snake venom. (C) 2009 Elsevier Ltd. All rights reserved.
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Palavras-chave
Bothrops (neuwiedi) pauloensis, Blood coagulation, Proteolytic enzymes, Serine proteinase, Thrombin-like enzymes
Como citar
Toxicon. Oxford: Pergamon-Elsevier B.V. Ltd, v. 54, n. 6, p. 725-735, 2009.