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Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom J. Venom. Anim. Toxins incl. Trop. Dis.
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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Subproteome of Lachesis muta rhombeata venom and preliminary studies on LmrSP-4, a novel snake venom serine proteinase J. Venom. Anim. Toxins incl. Trop. Dis.
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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