Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: 

RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 6
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys J. Venom. Anim. Toxins incl. Trop. Dis.
Ghorbanpur,M; Zare Mirakabadi,A; Zokaee,F; Zolfagarrian,H; Rabiei,H.
Agkistrodon halys is one of several dangerous snake species in Iran. Among the most important signs and symptoms in patients envenomated by this snake is disseminated intravascular coagulation. A thrombin-like enzyme, called AH143, was isolated from Agkistrodon halys venom by gel filtration on a Sephadex G-50 column, ion-exchange chromatography on a DEAE-Sepharose and high performance liquid chromatography (HPLC) on a C18 column. In the final stage of purification, 0.82 mg of purified enzyme was obtained from 182.5 mg of venom. The purified enzyme showed a single protein band by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), under reducing conditions, and its molecular mass was found to be about 30 kDa. AH143 revealed clotting...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Iranian snake; Venom; Agkistrodon halys; Serine protease; Chromatography; Coagulant activity.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992009000300005
Imagem não selecionada

Imprime registro no formato completo
Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities J. Venom. Anim. Toxins incl. Trop. Dis.
Megale,Ângela Alice Amadeu; Magnoli,Fábio Carlos; Kuniyoshi,Alexandre Kazuo; Iwai,Leo Kei; Tambourgi,Denise V.; Portaro,Fernanda C. V.; Silva,Wilmar Dias da.
Abstract Background: Bitis arietans is a venomous snake found in sub-Saharan Africa and in parts of Morocco and Saudi Arabia. The envenomation is characterized by local and systemic reactions including pain, blistering, edema and tissue damage, besides hemostatic and cardiovascular disturbances, which can cause death or permanent disabilities in its victims. However, the action mechanisms that provoke these effects remain poorly understood, especially the activities of purified venom components. Therefore, in order to elucidate the molecular mechanisms that make the Bitis arietans venom so potent and harmful to human beings, this study reports the isolation and biochemical characterization of a snake venom serine protease (SVSP). Methods: Solubilized...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bitis arietans; Venom; Antivenom; Serine protease; Fibrinogenolytic; Kinin-releasing activity.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100328
Imagem não selecionada

Imprime registro no formato completo
In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai J. Venom. Anim. Toxins incl. Trop. Dis.
Bae,Seong Kyeong; Lee,Hyunkyoung; Heo,Yunwi; Pyo,Min Jung; Choudhary,Indu; Han,Chang Hoon; Yoon,Won Duk; Kang,Changkeun; Kim,Euikyung.
Abstract Background: Because jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. Although the effects of their toxins are a matter of concern, information on the venom components, biological activity and pathological mechanisms are still scarce. Therefore, the aim of the present study was to investigate a serine protease component of Nemopilema nomurai jellyfish venom (NnV) and unveil its characteristics. Methods: To determine the relationship between fibrinolytic activity of NnV and the serine protease, fibrin zymography was performed using metalloprotease and serine protease inhibitors. The biochemical characterization of serine proteases of NnV were determined by the amidolytic assay. Fractions with...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Nemopilema nomurai; Jellyfish venom; Chymotrypsin; Serine protease; Fibrinolytic activity.
Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100323
Imagem não selecionada

Imprime registro no formato completo
Bothrops snake venoms and their isolated toxins, an L-amino acid oxidase and a serine protease, modulate human complement system pathways J. Venom. Anim. Toxins incl. Trop. Dis.
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
Imagem não selecionada

Imprime registro no formato completo
Native isolates of Trichoderma harzianum inducting resistance to Zymoseptoria tritici onwheat plants Boletín de la Sociedad
Stocco,Marina C; Mansilla,Andrea Y; Mónaco,Cecilia I; Segarra,Carmen; Lampugnani,Gladys; Abramoff,Cecilia; Marchetti,María F; Kripelz,Natalia; Cordo,Cristina C; Consolo,Verónica F.
Trichoderma harzianum inducting resistance to Zymoseptoria tritici. Septoria tritici blotch is endemic in the wheat growing cultivated areas of Argentina, which impacts in the crop yield. One management strategy is to use biocontrol agents. The objective of this work was to determine the effectiveness of Trichoderma spp. isolated from soils of different growing regions, as antagonist and characterize the T. harzianum effect throughout the proteolytic activity of the serine protease in the wheat plant. To determine the antagonistic capacities of Trichoderma spp. against Zimoseptoria tritici, wheat plants were grown from seeds coated with each of the ninety isolated Trichoderma. Antagonism was assessed 21 days after inoculation by the capacity of each...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Trichoderma harzianum; Biocontrol; Wheat; Septoria tritici blotch; ISR; Serine protease.
Ano: 2015 URL: http://www.scielo.org.ar/scielo.php?script=sci_arttext&pid=S1851-23722015000300002
Imagem não selecionada

Imprime registro no formato completo
Extracellular proteases of Halobacillus blutaparonensis strain M9, a new moderately halophilic bacterium BJM
Santos,Anderson F.; Valle,Roberta S.; Pacheco,Clarissa A.; Alvarez,Vanessa M.; Seldin,Lucy; Santos,André L.S..
Halophilic microorganisms are source of potential hydrolytic enzymes to be used in industrial and/or biotechnological processes. In the present study, we have investigated the ability of the moderately halophilic bacterium Halobacillus blutaparonensis (strain M9), a novel species described by our group, to release proteolytic enzymes. This bacterial strain abundantly proliferated in Luria-Bertani broth supplemented with 2.5% NaCl as well as secreted proteases to the extracellular environment. The production of proteases occurred in bacterial cells grown under different concentration of salt, ranging from 0.5% to 10% NaCl, in a similar way. The proteases secreted by H. blutaparonensis presented the following properties: (i) molecular masses ranging from 30...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Halobacillus blutaparonensis; Halophilic bacterium; Serine protease.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822013000400039
Registros recuperados: 6
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional