Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados BJMBR (2) Autor Arocha-Piñango,C.L. (1) Coll-Sangrona,E. (1) Couto,L.T. (1) Donato,J.L. (1) Nucci,G. de (1) Palavra-chave Plasmin (2) Clot lysis (1) Fibrinolysis (1) Lonomia achelous caterpillars (1) Plasminogen (1) Streptokinase (1) Substrate S-2251™ (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2004 (1) 1998 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Fibrinolytic action on fresh human clots of whole body extracts and two semipurified fractions from Lonomia achelous caterpillar BJMBR Coll-Sangrona,E.; Arocha-Piñango,C.L.. The severe bleeding diathesis produced by intoxication with the venom of Lonomia achelous caterpillars is characterized by prolonged bleeding from superficial skin wounds as well as massive hemorrhage into body cavities. The aim of the present study was to evaluate the effect of the crude venom and its fibrinolytic fractions on in vitro lysis of whole blood clots. Venom fractions with fibrinolytic activity were obtained by gel filtration chromatography on Sephadex G75 using imidazole buffer, pH 7.4, at a flow rate of 24 ml/h. Four peaks with fibrinolytic activity were obtained by this method. The highest activity was found in the first two peaks (both peaks were used for the experiments). The results show that the caterpillar venom degraded the preformed... Tipo: Info:eu-repo/semantics/article Palavras-chave: Lonomia achelous caterpillars; Fibrinolysis; Clot lysis; Plasmin. Ano: 1998 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998000600009 Analysis of five streptokinase formulations using the euglobulin lysis test and the plasminogen activation assay BJMBR Couto,L.T.; Donato,J.L.; Nucci,G. de. Streptokinase, a 47-kDa protein isolated and secreted by most group A, C and G ß-hemolytic streptococci, interacts with and activates human protein plasminogen to form an active complex capable of converting other plasminogen molecules to plasmin. Our objective was to compare five streptokinase formulations commercially available in Brazil in terms of their activity in the in vitro tests of euglobulin clot formation and of the hydrolysis of the plasmin-specific substrate S-2251™. Euglobulin lysis time was determined using a 96-well microtiter plate. Initially, human thrombin (10 IU/ml) and streptokinase were placed in individual wells, clot formation was initiated by the addition of plasma euglobulin, and turbidity was measured at 340 nm every 30 s. In the... Tipo: Info:eu-repo/semantics/article Palavras-chave: Streptokinase; Plasminogen; Plasmin; Substrate S-2251™. Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004001200015 Registros recuperados: 2 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