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	Provedor de dados 45 (1) 56 (1) Autor Quintilio,W. (2) Almeida,A.C. (1) Araujo,P.S. de (1) Brandi,I.V. (1) Cangussu,A.S.R. (1) Colen,F. (1) Costa,M.H.B. (1) Faljoni-Alário,A. (1) Lobato,F.C.F. (1) Sant'Anna,O.A. (1) Santos,H.O. (1) Sari,R.S. (1) Sobrinho,E.M. (1) Mais... Palavra-chave Adjuvant (1) Clostridiosis (1) Drug delivery system (1) Epsilon toxicoid (1) Hydrophobic modification (1) In vitro alternative method (1) Protein stability (1) Vaccine delivery system (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Info:eu-repo/semantics/other (1) Ano 2014 (1) 2002 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última ELISA and modified toxin-binding inhibition test for quality control of the clostridial vaccine processes 45 Sobrinho,E.M.; Almeida,A.C.; Brandi,I.V.; Colen,F.; Lobato,F.C.F.; Cangussu,A.S.R.; Santos,H.O.; Quintilio,W.; Sari,R.S.. This study aimed to assess and standardize the ELISA and modified ToBI test in vitro methods in order to verify the potency of epsilon toxicoid in comparison with the in vivo TCP method. The following epsilon toxoids were used: NIBSC standard from batches 375/07, 532/08, 551/08, 373/07 and 378/07. These were evaluated using a TCP test, ELISA and ToBI tests. The results indicate that the correlation ratio between the dilutions of standard NIBSC toxicoid and absorbance values of 89.44% obtained with the ELISA method support the use of the curve to evaluate epsilon toxoids. However, it was observed that the absorbance values were similar for all toxoids, thus presenting no significant difference between higher and lower concentration toxoids. For the ToBI... Tipo: Info:eu-repo/semantics/article Palavras-chave: Epsilon toxicoid; Clostridiosis; In vitro alternative method. Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0102-09352014000300713 The use of protein structure/activity relationships in the rational design of stable particulate delivery systems 56 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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