Please use this identifier to cite or link to this item:
- Molecular characterization of BjussuSP-I, a new thrombin-like enzyme with procoagulant and kallikrein-like activity isolated from Bothrops jararacussu snake venom
- Universidade de São Paulo (USP)
- Universidade Federal Fluminense (UFF)
- Universidade Federal do Rio de Janeiro (UFRJ)
- Universidade Estadual Paulista (UNESP)
- Univ Rondonia
- A thrombin-like enzyme, named BjussuSP-I, isolated from Bothrops jararacussu snake venom, is an acidic single-chain glycoprotein with M-r = 61,000, pI similar to 3.8 and 6% sugar. BjussuSP-I shows high proteolytic activity upon synthetic substrates, such as S-2238 and S-2288. It also shows procoagulant and kallikrein-like activity, but is unable to act on platelets and plasmin. These activities are inhibited by specific inhibitors of this class of enzymes. The complete cDNA sequence of BjussuSP-I with 696 bp encodes open reading frames of 232 amino acid residues, which conserve the common domains of thrombin-like serine proteases. BjussuSP-I shows a high structural homology with other thrombin-like enzymes from snake venoms where common amino acid residues are identified as those corresponding to the catalytic site and subsites S1, S2 and S3 already reported. In this study, we also demonstrated the importance of N-linked glycans, to improve thrombin-like activity of BjussuSP-I toxin. (c) 2007 Elsevier Masson SAS. All rights reserved.
- Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 90, n. 3, p. 500-507, 2008.
- Elsevier France-editions Scientifiques Medicales Elsevier
- thrombin-like enzyme
- Bothrops jararacussu
- snake venom
- proteolytic activity
- structural characterization
- Acesso restrito
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.