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  • Title: Biochemical and functional properties of a thrombin-like enzyme isolated from Bothrops pauloensis snake venom.
    Author: Costa FL, Rodrigues RS, Izidoro LF, Menaldo DL, Hamaguchi A, Homsi-Brandeburgo MI, Fuly AL, Soares SG, Selistre-de-Araújo HS, Barraviera B, Soares AM, Rodrigues VM.
    Journal: Toxicon; 2009 Nov; 54(6):725-35. PubMed ID: 19539638.
    Abstract:
    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 approximately 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.
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