Consulta: subjectFacets:"L-amino acid oxidase"
Registros recuperados: 5
Data/hora: 10/06/2024 10:17:46

Purification of an L-amino acid oxidase from Bungarus caeruleus (Indian krait) venom
Provedor de dados: Journal of Venomous Animals and Toxins Including Tropical Diseases
Autores: More,SS; Kiran,KM; Veena,SM; Gadag,JR.
Snake venoms are rich in enzymes such as phospholipase A2, proteolytic enzymes, hyaluronidases and phosphodiesterases, which are well characterized. However, L-amino acid oxidase (LAO EC.1.4.3.2) from snake venoms has not been extensively studied. A novel L-amino acid oxidase from Bungarus caeruleus venom was purified to homogeneity using a combination of ion-exchange by DEAE-cellulose chromatography and gel filtration on Sephadex® G-100 column. The purified monomer of LAO showed a molecular mass of 55 ±1 kDa estimated by SDS-PAGE. The specific activity of purified LAO was 6,230 ± 178 U/min/mg, versus 230 ± 3.0 U/min/mg for the whole desiccated venom, suggesting a 27-fold purification with a 25% yield. Optimal pH and temperature for maximum purified enzyme...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: L-amino acid oxidase; Bungarus caeruleus; Platelet aggregation.
Ano: 2010
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000100007

Purification and antibacterial activities of an L-amino acid oxidase from king cobra (Ophiophagus hannah) venom
Provedor de dados: Journal of Venomous Animals and Toxins Including Tropical Diseases
Autores: Phua,CS; Vejayan,J; Ambu,S; Ponnudurai,G; Gorajana,A.
Some constituents of snake venom have been found to display a variety of biological activities. The antibacterial property of snake venom, in particular, has gathered increasing scientific interest due to antibiotic resistance. In the present study, king cobra venom was screened against three strains of Staphylococcus aureus [including methicillin-resistant Staphylococcus aureus (MRSA)], three other species of gram-positive bacteria and six gram-negative bacteria. King cobra venom was active against all the 12 bacteria tested, and was most effective against Staphylococcus spp. (S. aureus and S. epidermidis). Subsequently, an antibacterial protein from king cobra venom was purified by gel filtration, anion exchange and heparin chromatography. Mass...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: L-amino acid oxidase; King cobra; Antibacterial activity; Ophiophagus hannah.
Ano: 2012
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000200010

Bothrops snake venoms and their isolated toxins, an L-amino acid oxidase and a serine protease, modulate human complement system pathways
Provedor de dados: Journal of Venomous Animals and Toxins Including Tropical Diseases
Autores: Ayres,Lorena Rocha; Récio,Alex dos Reis; Burin,Sandra Mara; Pereira,Juliana Campos; Martins,Andrea Casella; Sampaio,Suely Vilela; Castro,Fabíola Attié de; Pereira-Crott,Luciana Simon.
Background Activation of the complement system plays an important role in the regulation of immune and inflammatory reactions, and contributes to inflammatory responses triggered by envenomation provoked byBothrops snakes. The present study aimed to assess whether Bothrops jararacussuand Bothrops pirajai crude venoms and their isolated toxins, namely serine protease (BjussuSP-I) and L-amino acid oxidase (BpirLAAO-I), modulate human complement system pathways.Methods Lyophilized venom and toxin samples solubilized in phosphate buffered saline were diluted in appropriate buffers to evaluate their hemolytic activity on the alternative and classical pathways of the complement system. Venom- and toxin-treated normal human serum was added to the erythrocyte...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Bothrops jararacussu; Bothrops pirajai; Chemotaxis; Complement system; Kinetic microassay; L-amino acid oxidase; Serine protease; Snake venom.
Ano: 2015
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100336

Kinetic investigations and stability studies of two Bothrops L-amino acid oxidases
Provedor de dados: Journal of Venomous Animals and Toxins Including Tropical Diseases
Autores: 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

Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability
Provedor de dados: Journal of Venomous Animals and Toxins Including Tropical Diseases
Autores: 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