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1. | | MOREIRA, J. S.; OLIVEIRA, J. S.; BEMQUERER, M. P.; MACHADO-DE-ÁVILA, R. A.; SANTOS, D. M.; MATOS, D. C.; MARIA, B. T.; MAGALHÃES, P. P.; FARIAS, L. M. Purification of multifunctional substances active against Shigella sonnei. International Journal of Biological and Natural Sciences, v. 2, n. 5, p. 1-15, 2022. Biblioteca(s): Embrapa Gado de Leite. |
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Registros recuperados : 1 | |
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Registro Completo
Biblioteca(s): |
Embrapa Gado de Leite. |
Data corrente: |
01/12/2022 |
Data da última atualização: |
01/12/2022 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
C - 0 |
Autoria: |
MOREIRA, J. S.; OLIVEIRA, J. S.; BEMQUERER, M. P.; MACHADO-DE-ÁVILA, R. A.; SANTOS, D. M.; MATOS, D. C.; MARIA, B. T.; MAGALHÃES, P. P.; FARIAS, L. M. |
Afiliação: |
JAQUELINE S. MOREIRA, Universidade Federal de Minas Gerais; JAMIL S. OLIVEIRA, Universidade Federal de Minas Gerais; MARCELO PORTO BEMQUERER, CNPGL; RICARDO A. MACHADO-DE-ÁVILA, Universidade do Extremo Sul Catarinense; DANIEL M. SANTOS, Fundação Ezequiel Dias; DESIELLE C. MATOS, Universidade Federal de Minas Gerais; BRUNA T. MARIA, Universidade Federal de Minas Gerais; PAULA P. MAGALHÃES, Universidade Federal de Minas Gerais; LUIZ M. FARIAS, Universidade Federal de Minas Gerais. |
Título: |
Purification of multifunctional substances active against Shigella sonnei. |
Ano de publicação: |
2022 |
Fonte/Imprenta: |
International Journal of Biological and Natural Sciences, v. 2, n. 5, p. 1-15, 2022. |
Idioma: |
Inglês |
Conteúdo: |
Shigella is the etiological agent of shigellosis. Antimicrobial peptides and proteins are biologically active substances produced by prokaryotes and eukaryotes that may present antagonistic activity against a wide range of microorganism. In this study, the intracellular extract of a Shigella sonnei isolate was precipitated with 75% ammonium sulfate and purified by sequential chromatography steps using ion exchange, molecular exclusion, and reversed-phase columns. Analysis by mass spectrometry identified three substances with molecular masses of 7.2, 9.2 and 10.7 kDa, active against another Shigella sonnei isolate. The amino acid sequences of the active substances were evaluated with the aid of BLAST - P software. The antagonistic substances were identified, respectively, as 50S ribosomal protein L29 of Escherichia coli, DNA-binding protein HU-beta and ribosome hibernation promoting factor both of Shigella sonnei. Data demonstrated that Shigella sonnei synthesizes three antimicrobial substances that present other classical functions, active against another isolate of the same species. |
Thesagro: |
Bactéria; Doença; Peptídeo; Proteína; Shigella Sonnei. |
Categoria do assunto: |
H Saúde e Patologia |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1149041/1/Purification-of-multifunctional-substances-active-against-Shigella-sonnei.pdf
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Marc: |
LEADER 01898naa a2200277 a 4500 001 2149041 005 2022-12-01 008 2022 bl uuuu u00u1 u #d 100 1 $aMOREIRA, J. S. 245 $aPurification of multifunctional substances active against Shigella sonnei.$h[electronic resource] 260 $c2022 520 $aShigella is the etiological agent of shigellosis. Antimicrobial peptides and proteins are biologically active substances produced by prokaryotes and eukaryotes that may present antagonistic activity against a wide range of microorganism. In this study, the intracellular extract of a Shigella sonnei isolate was precipitated with 75% ammonium sulfate and purified by sequential chromatography steps using ion exchange, molecular exclusion, and reversed-phase columns. Analysis by mass spectrometry identified three substances with molecular masses of 7.2, 9.2 and 10.7 kDa, active against another Shigella sonnei isolate. The amino acid sequences of the active substances were evaluated with the aid of BLAST - P software. The antagonistic substances were identified, respectively, as 50S ribosomal protein L29 of Escherichia coli, DNA-binding protein HU-beta and ribosome hibernation promoting factor both of Shigella sonnei. Data demonstrated that Shigella sonnei synthesizes three antimicrobial substances that present other classical functions, active against another isolate of the same species. 650 $aBactéria 650 $aDoença 650 $aPeptídeo 650 $aProteína 650 $aShigella Sonnei 700 1 $aOLIVEIRA, J. S. 700 1 $aBEMQUERER, M. P. 700 1 $aMACHADO-DE-ÁVILA, R. A. 700 1 $aSANTOS, D. M. 700 1 $aMATOS, D. C. 700 1 $aMARIA, B. T. 700 1 $aMAGALHÃES, P. P. 700 1 $aFARIAS, L. M. 773 $tInternational Journal of Biological and Natural Sciences$gv. 2, n. 5, p. 1-15, 2022.
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Embrapa Gado de Leite (CNPGL) |
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