dc.creator | ANA, Carolina D. Sant | |
dc.creator | TICLI, Fabio K. | |
dc.creator | OLIVEIRA, Leandro L. | |
dc.creator | GIGLIO, Jose R. | |
dc.creator | RECHIA, Carem G. V. | |
dc.creator | FULY, Andre L. | |
dc.creator | ARAUJO, Heloisa S. Selistre de | |
dc.creator | FRANCO, Joao J. | |
dc.creator | STABELI, Rodrigo G. | |
dc.creator | SOARES, Andreimar M. | |
dc.creator | SAMPAIO, Suely V. | |
dc.date.accessioned | 2012-10-19T03:43:11Z | |
dc.date.accessioned | 2018-07-04T14:58:35Z | |
dc.date.available | 2012-10-19T03:43:11Z | |
dc.date.available | 2018-07-04T14:58:35Z | |
dc.date.created | 2012-10-19T03:43:11Z | |
dc.date.issued | 2008 | |
dc.identifier | COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY, v.151, n.3, Special Issue, p.443-454, 2008 | |
dc.identifier | 1095-6433 | |
dc.identifier | http://producao.usp.br/handle/BDPI/20259 | |
dc.identifier | 10.1016/j.cbpa.2007.02.036 | |
dc.identifier | http://dx.doi.org/10.1016/j.cbpa.2007.02.036 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1617043 | |
dc.description.abstract | A thrombin-like enzyme named BjussuSP-I, isolated from B. jararacussu snake venom, is an acidic single chain glycoprotein with approximately 6% sugar, Mr = 61,000 under reducing conditions and pI similar to 3.8, representing 1.09% of the chromatographic A(280) recovery. BjussuSP-I is a glycosylated scrine protease containing both N-linked carbohydrates and sialic acid in its structure. BjussuSP-I showed a high clotting activity upon human plasma, which was inhibited by PMSF, leupeptin, heparin and 1,10-phenantroline. This enzyme showed high stability regarding coagulant activity when analyzed at different temperatures (-70 to 37 degrees C), pHs (4.5 to 8.0), and presence of two divalent metal ions (Ca2+ and Mg2+). It also displayed TAME esterase and proteolytic activities toward natural (fibrinogen and fibrin) and synthetic (BAPNA) substrates, respectively, being also inhibited by PMSF and leupeptin. BjussuSP-I can induce production of polyclonal antibodies able to inhibit its clotting activity, but unable to inhibit its proteolytic activity on fibrinogen. The enzyme also showed crossed immunoreactivity against I I venom samples of Bothrops, I of Crotalus, and I of Calloselasma snakes, in addition of LAAO isolated from B. moojeni venom. It displayed neither hemorrhagic, myotoxic, edema-inducing profiles nor proteolytic activity on casein. BjussuSP-I showed an N-terminal sequence (VLGGDECDfNEHPFLA FLYS) similar to other thrombin-like enzymes from snake venoms. Based on its biochemical, enzymatic and pharmacological characteristics, BjussuSP-I was identified as a new thrombin-like enzyme isoform from Bothrops jararacussu snake venom. (C) 2007 Elsevier Inc. All rights reserved. | |
dc.language | eng | |
dc.publisher | ELSEVIER SCIENCE INC | |
dc.relation | Comparative Biochemistry and Physiology A-molecular & Integrative Physiology | |
dc.rights | Copyright ELSEVIER SCIENCE INC | |
dc.rights | restrictedAccess | |
dc.subject | Bothrops jararacussu | |
dc.subject | Snake venoms | |
dc.subject | Enzymatic characterization | |
dc.subject | Coagulation | |
dc.subject | Proteolysis | |
dc.subject | Thrombin-like enzyme | |
dc.subject | Polyclonal antibody | |
dc.title | BjussuSP-I: A new thrombin-like enzyme isolated from Bothrops jararacussu snake venom | |
dc.type | Artículos de revistas | |