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Pesquisa : G02.111.570.060.440 [Categoria DeCS]
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Texto completo SciELO Chile
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Id: lil-640538
Autor: Díaz, Mauricio; Venturini, Elena; Marchetti, Stefano; Arenas, Gloria; Marshall, Sergio H.
Título: Intein-mediated expression of cecropin in escherichia coli
Fonte: Electron. j. biotechnol;15(2):3-3, Mar. 2012. ilus, tab.
Idioma: en.
Projeto: Copec-UC foundation; . PBCT.
Resumo: 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, obtaining a final yield of 2.5 mg cecropin/l. Cecropin cleaved from the intein had its proper biologically active form, showing a micromolar antimicrobial activity against Vibrio ordalii, Vibrio alginolyticus and Escherichia coli.
Descritores: Antibacterianos/metabolismo
Escherichia coli
-Western Blotting
Cromatografia de Afinidade
Cromatografia Líquida de Alta Pressão
Clonagem Molecular
Fusão Gênica
Peptídeos Catiônicos Antimicrobianos/metabolismo
Proteínas Recombinantes
Limites: Humanos
Responsável: CL1.1 - Biblioteca Central

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Texto completo SciELO Brasil
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Id: lil-517016
Autor: Theodoro, Raquel Cordeiro; Bagagli, Eduardo.
Título: Inteins in pathogenic fungi: a phylogenetic tool and perspectives for therapeutic applications
Fonte: Mem. Inst. Oswaldo Cruz;104(3):497-504, May 2009. ilus.
Idioma: en.
Resumo: Inteins or "internal proteins" are coding sequences that are transcribed and translated with flanking sequences (exteins). After translation, the inteins are excised by an autocatalytic process and the host protein assumes its normal conformation and develops its expected function. These parasitic genetic elements have been found in important, conserved proteins in all three domains of life. Most of the eukaryotic inteins are present in the fungi kingdom and the PRP8 intein is one of the most widespread inteins, occurring in important pathogens such as Cryptococcus neoformans (varieties grubii and neoformans), Cryptococcus gattii, Histoplasma capsulatum and Paracoccidioides brasiliensis. The knowledge of conserved and non-conserved domains in inteins have opened up new opportunities for the study of population variability in pathogenic fungi, including their phylogenetic relationships and recognition or diagnoses of species. Furthermore, inteins in pathogenic fungi should also be considered a promising therapeutic drug target, since once the autocatalytic splicing is inhibited, the host protein, which is typically vital, will not be able to perform its normal function and the fungal cell will not survive or reproduce.
Descritores: Cryptococcus/genética
Responsável: BR1.1 - BIREME

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Texto completo SciELO Brasil
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Id: lil-494527
Autor: Matroudi, S; Zamani, M. R; Motallebi, M.
Título: Molecular cloning of chitinase 33 (chit33) gene from Trichoderma atroviride / Clonagem molecular do gene quitinase 33 (chit33) em Trichoderma atroviride
Fonte: Braz. j. microbiol;39(3):433-437, July-Sept. 2008. ilus, tab.
Idioma: en.
Resumo: In this study Trichoderma atroviride was selected as over producer of chitinase enzyme among 30 different isolates of Trichoderma sp. on the basis of chitinase specific activity. From this isolate the genomic and cDNA clones encoding chit33 have been isolated and sequenced. Comparison of genomic and cDNA sequences for defining gene structure indicates that this gene contains three short introns and also an open reading frame coding for a protein of 321 amino acids. The deduced amino acid sequence includes a 19 aa putative signal peptide. Homology between this sequence and other reported Trichoderma Chit33 proteins are discussed. The coding sequence of chit33 gene was cloned in pEt26b(+) expression vector and expressed in E. coli.

Neste estudo Trichoderma atroviride foi escolhido como superprodutor da enzima quitinase dentre 30 isolados de Trichoderma sp. com base na atividade específica de quitinase. Clones de cDNA e genômico codificando chit33 foram obtidos deste isolado e seqüenciados. A comparação das seqüências genômica e de cDNA para definir a estrutura do gene indicou que este contém três pequenos introns e uma fase aberta de leitura codificando uma proteína de 321 aminoácidos. A seqüência de aminoácidos deduzida inclui um possível peptídio sinal de 19 aminoácidos. Homologia entre esta seqüência e outras proteínas Chit33 descritas de Trichoderma é discutida. A seqüência codificadora do gene chit33 foi clonada no vetor de expressão pET26b(+) e expressa em E. coli.
Descritores: Clonagem Molecular
Técnicas In Vitro
Trichoderma/isolamento & purificação
-Sequência de Aminoácidos
Estrutura Molecular
Tipo de Publ: Estudo Comparativo
Responsável: BR32.1 - Serviço de Biblioteca e Informação Biomédica

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