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	Provedor de dados Colegio de Postgraduados (1) BJM (1) J. Venom. Anim. Toxins incl. Trop. Dis. (1) Autor Branquinha,Marta Helena (1) Chaia,André Adriano (1) Costa,J. O. (1) García Hernández, Claudia (1) Giovanni-De-Simone,Salvatore (1) Hamaguchi,A. (1) Homsi-Brandeburgo,M. I. (1) Lima,Ana Paula Cabral de Araújo (1) Oliveira,C. Z. (1) Oliveira,F. (1) Petinate,Simone Dias Gonçalves (1) Petric,C. B. (1) Soares,A. M. (1) Vermelho,Alane Beatriz (1) Mais... Palavra-chave Metalloproteases (3) Bothrops alternatus (1) Brevundimonas diminuta (1) Cocoa (1) Defibrinogenation in vivo (1) Extracellular proteases (1) Fibrinogenolytic activity (1) Frosty pod rot (1) Functional characterization (1) Maestría (1) Metaloproteasas (1) Moniliasis (1) Moniliophthora roreri (1) Producción Agroalimentaria en el Trópico (1) Proteasas (1) Proteasas secretadas (1) Proteases (1) Pseudomonadaceae (1) Secreted proteases (1) Snake venom (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Tesis (1) Ano 2007 (2) 2000 (1) País Brazil (2) Mexico (1) Idioma Inglês (2) Espanhol (1)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Caracterización del sistema proteolítico de Moniliophthora roreri (Cif.) Evans et al., causante de la moniliasis del cacao Colegio de Postgraduados García Hernández, Claudia. El presente trabajo constituye el primer reporte sobre el estudio del sistema proteolítico del hongo Moniliophthora roreri, agente causal de la moniliasis del cacao. El trabajo inició con la identificación de la cepa aislada a partir de frutos de cacao infectados. La amplificación y secuenciación de un fragmento del gen 18S rDNA, permitió la identificación molecular de la cepa aislada como M. roreri, designada como MRO1. A continuación, se evaluó el crecimiento celular de M. roreri en los medios de cultivo líquidos mineral y V8 enriquecido, indicando que en este último se obtiene mayor peso seco en mg mL-1. La determinación de los niveles de las actividades proteolíticas de aspartil proteasa (mrAP), aminopeptidasa (mrAPE), carboxipeptidasa (mrCP) y... Tipo: Tesis Palavras-chave: Moniliophthora roreri; Moniliasis; Proteasas; Proteasas secretadas; Metaloproteasas; Maestría; Producción Agroalimentaria en el Trópico; Cocoa; Frosty pod rot; Proteases; Secreted proteases; Metalloproteases. Ano: 2007 URL: http://hdl.handle.net/10521/1252 Purification and functional characterization of two fibrinogenolytic enzymes from Bothrops alternatus venom J. Venom. Anim. Toxins incl. Trop. Dis. Costa,J. O.; Petric,C. B.; Hamaguchi,A.; Homsi-Brandeburgo,M. I.; Oliveira,C. Z.; Soares,A. M.; Oliveira,F.. Two fibrinogenolytic enzymes, Bothrops alternatus metalloprotease isoform (BaltMP)-I and II, were purified from Bothrops alternatus venom using Diethylaminoethyl (DEAE) Sephacel, Sephadex G-75 and Heparin-Agarose column chromatography. Purified BaltMP-I and II ran as single protein bands on analytical polyacrylamide gel electrophoresis and showed molecular weights of 29000 and 36000, respectively, under reducing conditions in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). BaltMP-II, but not BaltMP-I, displayed blood-clotting activity in bovine plasma, which was about 10-fold higher than that of the crude venom. Both enzymes were proteolytically active against bovine fibrinogen as substrate. When fibrinogen and each enzyme were... Tipo: Info:eu-repo/semantics/article Palavras-chave: Snake venom; Bothrops alternatus; Metalloproteases; Functional characterization; Fibrinogenolytic activity; Defibrinogenation in vivo. Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000300007 Identification and properties of two extracellular proteases from Brevundimonas diminuta BJM Chaia,André Adriano; Giovanni-De-Simone,Salvatore; Petinate,Simone Dias Gonçalves; Lima,Ana Paula Cabral de Araújo; Branquinha,Marta Helena; Vermelho,Alane Beatriz. Extracellular proteases from Brevundimonas diminuta (syn. Pseudomonas diminuta) were studied in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) containing a copolymerized substrate. Two proteases were detected migrating at 67 kDa and 50 kDa: both of them hydrolysed preferentially gelatin, but casein was also degraded and a slight hydrolysis was observed with hemoglobin. No detectable extracellular proteolytic activity was found in bovine serum albumin-containing gels. The optima temperature and pH for proteolytic activity were between 40ºC and 50ºC in a pH ranging from 7.0 to 11.0, respectively. These enzymes were isolated by analytical high performance liquid chromatography (HPLC). Protease assays with the synthetic substrate... Tipo: Info:eu-repo/semantics/article Palavras-chave: Metalloproteases; Brevundimonas diminuta; Pseudomonadaceae; Extracellular proteases. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822000000100007 Registros recuperados: 3 Primeira ... 1 ... Última

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