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Biological characterization of compounds from Rhinella schneideri poison that act on the complement system J. Venom. Anim. Toxins incl. Trop. Dis.
Anjolette,Fernando A. P.; Leite,Flávia P.; Bordon,Karla C. F.; Azzolini,Ana Elisa C. S; Pereira,Juliana C.; Pereira-Crott,Luciana S.; Arantes,Eliane C..
Background The skin secretions of toads of the family Bufonidae contain biogenic amines, alkaloids, steroids (bufotoxins), bufodienolides (bufogenin), peptides and proteins. The poison of Rhinella schneideri, formerly classified as Bufo paracnemis, presents components that act on different biological systems, including the complement system. The aim of this study was to isolate and examine the activity ofRhinella schneideri poison (RsP) components on the complement system.Methods The components active on the complement system were purified in three chromatographic steps, using a combination of cation-exchange, anion-exchange and gel filtration chromatography. The resulting fractions were analyzed by SDS-PAGE and screened for their activity in the hemolytic...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Complement system; Hemolytic activity; Neutrophil chemotaxis; Rhinella schneideri; Terminal complement complex (SC5b-9); Toad poison.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100334
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Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability J. Venom. Anim. Toxins incl. Trop. Dis.
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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Partial purification and functional characterization of Ts19 Frag-I, a novel toxin from Tityus serrulatus scorpion venom J. Venom. Anim. Toxins incl. Trop. Dis.
Lima,Priscila C.; Bordon,Karla C. F.; Pucca,Manuela B.; Cerni,Felipe A.; Zoccal,Karina F.; Faccioli,Lucia H.; Arantes,Eliane C..
Abstract Background The yellow scorpion Tityus serrulatus (Ts) is responsible for the highest number of accidents and the most severe scorpion envenoming in Brazil. Although its venom has been studied since the 1950s, it presents a number of orphan peptides that have not been studied so far. The objective of our research was to isolate and identify the components present in the fractions VIIIA and VIIIB of Ts venom, in order to search for a novel toxin. The major isolated toxins were further investigated for macrophage modulation. Methods The fractions VIIIA and VIIIB, obtained from Ts venom cation exchange chromatography, were rechromatographed on a C18 column (4.6 × 250 mm) followed by a reversed-phase chromatography using another C18 column (2.1 ×...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Β-KTx; Cytokine; Interleukin; Neurotoxin; Pro-inflammatory; Scorpion venom; Tityus serrulatus.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100353
Registros recuperados: 3
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