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| Bordon,Karla C. F.; Wiezel,Gisele A.; Cabral,Hamilton; Arantes,Eliane C.. |
| BackgroundCrotalus durissus terrificus venom (CdtV) is one of the most studied snake venoms in Brazil. Despite presenting several well known proteins, its L-amino acid oxidase (LAAO) has not been studied previously. This study aimed to isolate, characterize and evaluate the enzyme stability of bordonein-L, an LAAO from CdtV.Methods The enzyme was isolated through cation exchange, gel filtration and affinity chromatography, followed by a reversed-phase fast protein liquid chromatography to confirm its purity. Subsequently, its N-terminal amino acid sequence was determined by Edman degradation. The enzyme activity and stability were evaluated by a microplate colorimetric assay and the molecular mass was estimated by SDS-PAGE using periodic acid-Schiff... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Crotalus durissus terrificus; L-amino acid oxidase; Rattlesnake; Enzyme activity; Enzyme stability; Chromatography; Snake venom; Yellow venom; Stabilization. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100335 |
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| Costa,Tássia R.; Carone,Sante E. I.; Tucci,Luiz F. F.; Menaldo,Danilo L.; Rosa-Garzon,Nathalia G.; Cabral,Hamilton; Sampaio,Suely V.. |
| Abstract Background: L-amino acid oxidases isolated from snake venoms (SV-LAAOs) are enzymes that have great therapeutic potential and are currently being investigated as tools for developing new strategies to treat various diseases, including cancer and bacterial infections. The main objective of this study was to make a brief evaluation of the enzymatic stability of two Bothrops LAAOs, one isolated from Bothrops jararacussu (BjussuLAAO-II) and the other from Bothrops moojeni (BmooLAAO-I) venoms. Methods and results: The enzymatic activity and stability of both LAAOs were evaluated by microplate colorimetric assays, for which BjussuLAAO-II and BmooLAAO-I were incubated with different L-amino acid substrates, in the presence of different ions, and at... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Snake venom; Bothrops; L-amino acid oxidase; Enzymatic stability. |
| Ano: 2018 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100327 |
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| Mateus,Rogério Pincela; Cabral,Hamilton; Bonilla-Rodriguez,Gustavo Orlando; Ceron,Carlos Roberto. |
| A method that allows the measure of molecular weight of two well-known and closely related esterases from Drosophila mojavensis and its sibling species, D. arizonae, is here described, using native polyacrylamide gel electrophoresis at several concentrations, applying Fergunson´s principles. These enzymes, namely EST-4 and EST-5, presented molecular weight values between 81 and 91 kDa. In spite of their distinct expression pattern through the insect's life cycle, they showed properties of isoenzymes codified by distinct structural genes, supporting the hypothesis of a rather recent gene duplication event that generated both in D. mojavensis and D. arizonae, as well as in other species of repleta group. The method is simple and adequate to be applied to... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Esterases; Isoenzymes; Molecular weight determination; Drosophila mojavensis; Drosophila arizonae; PAGE. |
| Ano: 2009 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132009000500004 |
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| Cordeiro,Francielle Almeida; Coutinho,Bárbara Marques; Wiezel,Gisele Adriano; Bordon,Karla de Castro Figueiredo; Bregge-Silva,Cristiane; Rosa-Garzon,Nathalia Gonsales; Cabral,Hamilton; Ueberheide,Beatrix; Arantes,Eliane Candiani. |
| Abstract Background: Lachesis muta rhombeata (Lmr) is the largest venomous snake in Latin America and its venom contains mainly enzymatic components, such as serine and metalloproteases, L-amino acid oxidase and phospholipases A2. Metalloproteases comprise a large group of zinc-dependent proteases that cleave basement membrane components such as fibronectin, laminin and collagen type IV. These enzymes are responsible for local and systemic changes, including haemorrhage, myonecrosis and inflammation. This study aimed the isolation and enzymatic characterization of the first metalloprotease (Lmr-MP) from Lmr venom (LmrV). Methods and results: Lmr-MP was purified through two chromatographic steps and submitted to enzymatic characterization. It showed... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Lachesis muta rhombeata; Metalloprotease; Proteases; Snake venom. |
| Ano: 2018 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100323 |
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| Wiezel,Gisele A; Bordon,Karla CF; Silva,Ronivaldo R; Gomes,Mário SR; Cabral,Hamilton; Rodrigues,Veridiana M; Ueberheide,Beatrix; Arantes,Eliane C. |
| Abstract Background: Lachesis muta rhombeata is one of the venomous snakes of medical importance in Brazil whose envenoming is characterized by local and systemic effects which may produce even shock and death. Its venom is mainly comprised of serine and metalloproteinases, phospholipases A2 and bradykinin-potentiating peptides. Based on a previously reported fractionation of L. m. rhombeata venom (LmrV), we decided to perform a subproteome analysis of its major fraction and investigated a novel component present in this venom. Methods: LmrV was fractionated through molecular exclusion chromatography and the main fraction (S5) was submitted to fibrinogenolytic activity assay and fractionated by reversed-phase chromatography. The N-terminal sequences of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bushmaster; Snake venom; SVSP; Kallikrein-like; Plasminogen activator; Kininogenase; Lectin; Protease; Envenomation. |
| Ano: 2019 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992019000100307 |
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