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	Provedor de dados BJMBR (2) Autor Sant'Anna,O.A. (2) Araujo,P.S. de (1) Costa,M.H.B. (1) Faljoni-Alário,A. (1) Flangini,M. (1) Ibañez,O.M. (1) Martins,G.A. (1) Quintilio,W. (1) Rizzo,L.V. (1) Vieira de Moraes,L. (1) Mais... Palavra-chave Adjuvant (1) Autoimmunity (1) Drug delivery system (1) Genetically selected mice (1) Hydrophobic modification (1) IgG1 and IgG2a isotypes (1) Inflammation (1) Protein stability (1) Uveitis (1) Vaccine delivery system (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Info:eu-repo/semantics/other (1) Ano 2006 (1) 2002 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última The anti-IRBP IgG1 and IgG2a response does not correlate with susceptibility to experimental autoimmune uveitis BJMBR Vieira de Moraes,L.; Martins,G.A.; Flangini,M.; Ibañez,O.M.; Sant'Anna,O.A.; Rizzo,L.V.. Susceptibility to experimental autoimmune uveitis (EAU) in inbred mice has been associated with a dominant Th1 response. Elevated anti-inter-photoreceptor retinoid-binding protein (anti-IRBP) IgG2a/IgG1 antibody ratios have been implicated as candidate markers to predict disease severity. In the present study, both the anti-IRBP antibody isotype and severity of EAU phenotypes were examined in 4 non-isogenic genetically selected mouse lines to determine if they can be used as general markers of disease. Mice between 8 and 12 weeks old selected for high (H III) or low (L III) antibody response and for maximum (AIR MAX) or minimum (AIR MIN) acute inflammatory reaction (AIR) were immunized with IRBP. Each experiment was performed with at least 5 mice per... Tipo: Info:eu-repo/semantics/article Palavras-chave: Autoimmunity; IgG1 and IgG2a isotypes; Inflammation; Genetically selected mice; Uveitis. Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2006000600010 The use of protein structure/activity relationships in the rational design of stable particulate delivery systems BJMBR Costa,M.H.B.; Quintilio,W.; Sant'Anna,O.A.; Faljoni-Alário,A.; Araujo,P.S. de. The recombinant heat shock protein (18 kDa-hsp) from Mycobacterium leprae was studied as a T-epitope model for vaccine development. We present a structural analysis of the stability of recombinant 18 kDa-hsp during different processing steps. Circular dichroism and ELISA were used to monitor protein structure after thermal stress, lyophilization and chemical modification. We observed that the 18 kDa-hsp is extremely resistant to a wide range of temperatures (60% of activity is retained at 80ºC for 20 min). N-Acylation increased its ordered structure by 4% and decreased its ß-T1 structure by 2%. ELISA demonstrated that the native conformation of the 18 kDa-hsp was preserved after hydrophobic modification by acylation. The recombinant 18 kDa-hsp resists to a... Tipo: Info:eu-repo/semantics/other Palavras-chave: Protein stability; Hydrophobic modification; Vaccine delivery system; Drug delivery system; Adjuvant. Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000600014 Registros recuperados: 2 Primeira ... 1 ... Última

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