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	Provedor de dados Electron. J. Biotechnol. (4) Autor Marshall,Sergio H (4) Arenas,Gloria (3) Díaz,Mauricio (2) Mercado,Luis (2) Guzmán,Fanny (1) Marchetti,Stefano (1) Rojas,Verónica (1) Schmitt,Paulina (1) Valenzuela,Cristián (1) Venturini,Elena (1) Mais... Palavra-chave Antimicrobial peptides (2) Antibody (1) Antimicrobial (1) Biochemical characterization (1) Caspase-3 (1) Cecropin (1) Escherichia coli (1) Expression (1) Fish apoptosis (1) Fusion (1) Gill tissues (1) In vitro activity (1) Intein (1) Mussels (1) Peptide (1) Piscirickettsia salmonis (1) Soluble (1) Mais... Tipo do documento Journal article (4) Ano 2012 (2) 2008 (1) 2005 (1) País Chile (4) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última Intein-mediated expression of cecropin in Escherichia coli Electron. J. Biotechnol. Díaz,Mauricio; Venturini,Elena; Marchetti,Stefano; Arenas,Gloria; Marshall,Sergio H. Different strategies have been used to overcome the difficulties to produce antimicrobial peptides. Here we used Intein Mediated Purification with an Affinity Chitin-binding Tag (IMPACT-System, New England Biolabs) for the expression of the antimicrobial peptide cecropin to reduce its sensitivity to intracellular proteases and use its inducible self-cleaving capability to remove the carrier. Cecropin was cloned into suitable expression vector pTYB11, and expression induced by IPTG in Escherichia coli ER2566. The use of 22ºC induction allowed the expression of cecropin with its intein carrier in soluble form. Cell extracts were purified by chitin affinity chromatography and intein-mediated splicing of the target protein was achieved by thiol addition,... Tipo: Journal article Palavras-chave: Antimicrobial; Cecropin; Fusion; Intein; Peptide; Soluble. Ano: 2012 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582012000200003 Design and expression of a retro doublet of cecropin with enhanced activity Electron. J. Biotechnol. Díaz,Mauricio; Arenas,Gloria; Marshall,Sergio H. Novel doublet molecules of cecropin A from Drosophila melanogaster were designed and constructed combining the regular (CECdir) with the inverted (CECret) coding sequence of the standard CEC A1 gene resulting in the following configurations: CECdir-CECret and CECret-CECdir. These two recombinant molecules were generated using a three-primer driven PCR reaction yielding composite single functional aminoacidic molecules with the coding sequences of CECdir linked in frame with the coding sequence of CECret and vice versa. In order to obtain these constructions, a retropeptide DNA-coding sequence was chemically synthesized to match the expected polarity of the newly generated CECret sequence. Both doublet antimicrobial peptides (drAMPs) were cloned in the T7... Tipo: Journal article Palavras-chave: Antimicrobial peptides; Escherichia coli; Expression. Ano: 2008 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582008000200006 Development of a caspase-3 antibody as a tool for detecting apoptosis in cells from rainbow trout (Oncorhynchus mykiss) Electron. J. Biotechnol. Rojas,Verónica; Guzmán,Fanny; Valenzuela,Cristián; Marshall,Sergio H; Mercado,Luis. Background: Apoptosis is an active cell death process mediated by caspases activation, in which different extrinsic or intrinsic signalling pathways result in direct activation of effector caspases. Caspase-3 is considered to be the most important of the executioner caspases, which cause the morphological and biochemical changes detected in apoptotic cells. Different bacterial and virus pathogens have developed different strategies to survive inside the host and overcome natural protections, one of them is inducing apoptotic death in infected cells. We have demonstrated previously that Piscirickettsia salmonis activates this process in monocytes/macrophages from salmonid RTS11 cell line both by morphological and caspase detection assays; nevertheless,... Tipo: Journal article Palavras-chave: Antibody; Caspase-3; Fish apoptosis; Piscirickettsia salmonis. Ano: 2012 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582012000500012 Gill tissues of the mussel Mytilus edulis chilensis: A new source for antimicrobial peptides Electron. J. Biotechnol. Mercado,Luis; Schmitt,Paulina; Marshall,Sergio H; Arenas,Gloria. Antimicrobial peptides are small-sized, cationic and amphipathic molecules able to neutralize pathogenic microorganisms. Their antimicrobial effects tie them to mechanisms of immune defense, which is why they have been normally purified from immune cells. We describe an apparently new group of antimicrobial peptides from gill tissues of the mussel Mytilus edulis chilensis. 20 specimens yielded 40 g of gills which produced 16 mg of an enriched fraction with antimicrobial activity as low as 0.045 µg/µl over reference strains. Considering the chemical nature of these molecules we used an acid extraction procedure followed by consecutive cationic exchange and hydrophobic interaction chromatography steps for peptide enrichment. The resulting... Tipo: Journal article Palavras-chave: Antimicrobial peptides; Biochemical characterization; Gill tissues; In vitro activity; Mussels. Ano: 2005 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582005000300008 Registros recuperados: 4 Primeira ... 1 ... Última

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