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Registro Completo |
Biblioteca(s): |
Embrapa Gado de Corte; Embrapa Unidades Centrais. |
Data corrente: |
18/04/1998 |
Data da última atualização: |
18/04/1998 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
MIRANDA, C. H. B.; SEIFFERT, N. F.; SOUTO, S. M. |
Afiliação: |
CNPGC. |
Título: |
Especificidade e competitividade de estirpes de Rhizobium em centrosema sob condicoes controladas. |
Ano de publicação: |
1985 |
Fonte/Imprenta: |
Pesquisa Agropecuaria Brasileira, Brasilia, v.20, n.10, p.1157-1161, out. 1985. |
Idioma: |
Português |
Conteúdo: |
Foram conduzidos dois experimentos em casa-de-vegetacao, em areia-vermiculita, com a finalidade de comparar a eficiencia e especificidade entre onze estirpes de Rhizobium e tres centrosemas - Centrosema sp GC 372/79. Centrosema sp (hibrido interespecifico Itaguai) e C. macrocarpum CIAT 5065- e identificar a estirpe de Rhizobium responsavel pela formacao de nodulos no hibrido Itaguai quando feita inoculacao com mistura de estirpes. A estirpe C-106, isolada de C. pubescens, apresentou peso de nodulo, N-total e eficiencia relativa significativamente maiores (p<0,05) do que as demais estirpes. Entretanto, mostrou-se incapaz de formar nodulos quando inoculada junto com a estirpe C-551, isolada igualmente de C. pubescens, ou formou pequena percentagem de nodulos quando em mistura com outras duas estirpes. A estirpe C-551 mostrou-se pouco eficiente, mas altamente competitiva, sendo capaz de formar de 70% a 100% dos nodulos quando inoculada em conjunto com outras tres estirpes. Dentre os materiais estudados, o hibrido Itaguai apresentou melhor peso de nodulos, producao de materia seca e N total. |
Palavras-Chave: |
Biological differences; Fixacao biologica de N2; Forrage legumes; Inoculation; Leguminosas forrageiras; Nodes. |
Thesagro: |
Centrosema; Estirpe; Inoculação; Microbiologia; Nódulo; Rhizobium. |
Thesaurus Nal: |
microbiology; nitrogen fixation. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/203857/1/Especificidade-e-competitividade-de-estipes.pdf
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Marc: |
LEADER 01997naa a2200313 a 4500 001 1104611 005 1998-04-18 008 1985 bl uuuu u00u1 u #d 100 1 $aMIRANDA, C. H. B. 245 $aEspecificidade e competitividade de estirpes de Rhizobium em centrosema sob condicoes controladas. 260 $c1985 520 $aForam conduzidos dois experimentos em casa-de-vegetacao, em areia-vermiculita, com a finalidade de comparar a eficiencia e especificidade entre onze estirpes de Rhizobium e tres centrosemas - Centrosema sp GC 372/79. Centrosema sp (hibrido interespecifico Itaguai) e C. macrocarpum CIAT 5065- e identificar a estirpe de Rhizobium responsavel pela formacao de nodulos no hibrido Itaguai quando feita inoculacao com mistura de estirpes. A estirpe C-106, isolada de C. pubescens, apresentou peso de nodulo, N-total e eficiencia relativa significativamente maiores (p<0,05) do que as demais estirpes. Entretanto, mostrou-se incapaz de formar nodulos quando inoculada junto com a estirpe C-551, isolada igualmente de C. pubescens, ou formou pequena percentagem de nodulos quando em mistura com outras duas estirpes. A estirpe C-551 mostrou-se pouco eficiente, mas altamente competitiva, sendo capaz de formar de 70% a 100% dos nodulos quando inoculada em conjunto com outras tres estirpes. Dentre os materiais estudados, o hibrido Itaguai apresentou melhor peso de nodulos, producao de materia seca e N total. 650 $amicrobiology 650 $anitrogen fixation 650 $aCentrosema 650 $aEstirpe 650 $aInoculação 650 $aMicrobiologia 650 $aNódulo 650 $aRhizobium 653 $aBiological differences 653 $aFixacao biologica de N2 653 $aForrage legumes 653 $aInoculation 653 $aLeguminosas forrageiras 653 $aNodes 700 1 $aSEIFFERT, N. F. 700 1 $aSOUTO, S. M. 773 $tPesquisa Agropecuaria Brasileira, Brasilia$gv.20, n.10, p.1157-1161, out. 1985.
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Registro original: |
Embrapa Unidades Centrais (AI-SEDE) |
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Registro Completo
Biblioteca(s): |
Embrapa Milho e Sorgo. |
Data corrente: |
17/12/2018 |
Data da última atualização: |
18/02/2019 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 1 |
Autoria: |
SILVA, I. H. S. da; GOMÉZ, I.; SÁNCHEZ, J.; CASTRO, D. L. M. de; VALICENTE, F. H.; SOBERÓN, M.; POLANCZYK, R. A.; BRAVO, A. |
Afiliação: |
Igor Henrique Sena da Silva, Universidade Estadual Paulista; Isabel Goméz, Universidad Nacional Autónoma de México; Jorge Sánchez, Universidad Nacional Autónoma de México; Diana L. Martínez de Castro, Universidad Nacional Autónoma de México; FERNANDO HERCOS VALICENTE, CNPMS; Mario Soberón, Universidad Nacional Autónoma de México; Ricardo Antonio Polanczyk, Universidade Estadual Paulista; Alejandra Bravo, Universidad Nacional Autónoma de México. |
Título: |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin. |
Ano de publicação: |
2018 |
Fonte/Imprenta: |
Plos One, San Francisco, v. 13, n. 12, e0207789, 2018. |
DOI: |
10.1371/journal.pone.0207789 |
Idioma: |
Inglês |
Conteúdo: |
Helicoverpa armigera is a polyphagous pest sensitive to Cry1Ac protein from Bacillus thuringiensis (Bt). The susceptibility of the different larval instars of H. armigera to Cry1Ac protoxin showed a significant 45-fold reduction in late instars compared to early instars. A possible hypothesis is that gut surface proteins that bind to Cry1Ac differ in both instars, although higher Cry toxin degradation in late instars could also explain the observed differences in susceptibility. Here we compared the Cry1Ac-binding proteins from second and fifth instars by pull-down assays and liquid chromatography coupled to mass spectrometry analysis (LC-MS/MS). The data show differential protein interaction patterns of Cry1Ac in the two instars analyzed. Alkaline phosphatase, and other membrane proteins, such as prohibitin and an anion selective channel protein were identified only in the second instar, suggesting that these proteins may be involved in the higher toxicity of Cry1Ac in early instars of H. armigera. Eleven Cry1Ac binindg proteins were identified exclusively in late instar larvae, like different proteases such as trypsin-like protease, azurocidin-like proteinase, and carboxypeptidase. Different aminopeptidase N isofroms were identified in both instar larvae. We compared the Cry1Ac protoxin degradation using midgut juice from late and early instars, showing that the midgut juice from late instars is more efficient to degrade Cry1Ac protoxin than that of early instars, suggesting that increased proteolytic activity on the toxin could also explain the low Cry1Ac toxicity in late instars. MenosHelicoverpa armigera is a polyphagous pest sensitive to Cry1Ac protein from Bacillus thuringiensis (Bt). The susceptibility of the different larval instars of H. armigera to Cry1Ac protoxin showed a significant 45-fold reduction in late instars compared to early instars. A possible hypothesis is that gut surface proteins that bind to Cry1Ac differ in both instars, although higher Cry toxin degradation in late instars could also explain the observed differences in susceptibility. Here we compared the Cry1Ac-binding proteins from second and fifth instars by pull-down assays and liquid chromatography coupled to mass spectrometry analysis (LC-MS/MS). The data show differential protein interaction patterns of Cry1Ac in the two instars analyzed. Alkaline phosphatase, and other membrane proteins, such as prohibitin and an anion selective channel protein were identified only in the second instar, suggesting that these proteins may be involved in the higher toxicity of Cry1Ac in early instars of H. armigera. Eleven Cry1Ac binindg proteins were identified exclusively in late instar larvae, like different proteases such as trypsin-like protease, azurocidin-like proteinase, and carboxypeptidase. Different aminopeptidase N isofroms were identified in both instar larvae. We compared the Cry1Ac protoxin degradation using midgut juice from late and early instars, showing that the midgut juice from late instars is more efficient to degrade Cry1Ac protoxin than that of early instars, suggesti... Mostrar Tudo |
Thesagro: |
Praga de Planta; Proteína; Toxina. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/188667/1/Identification-midgut.pdf
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Marc: |
LEADER 02401naa a2200253 a 4500 001 2101792 005 2019-02-18 008 2018 bl uuuu u00u1 u #d 024 7 $a10.1371/journal.pone.0207789$2DOI 100 1 $aSILVA, I. H. S. da 245 $aIdentification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera$bNoctuidae) that bind to Cry1Ac toxin.$h[electronic resource] 260 $c2018 520 $aHelicoverpa armigera is a polyphagous pest sensitive to Cry1Ac protein from Bacillus thuringiensis (Bt). The susceptibility of the different larval instars of H. armigera to Cry1Ac protoxin showed a significant 45-fold reduction in late instars compared to early instars. A possible hypothesis is that gut surface proteins that bind to Cry1Ac differ in both instars, although higher Cry toxin degradation in late instars could also explain the observed differences in susceptibility. Here we compared the Cry1Ac-binding proteins from second and fifth instars by pull-down assays and liquid chromatography coupled to mass spectrometry analysis (LC-MS/MS). The data show differential protein interaction patterns of Cry1Ac in the two instars analyzed. Alkaline phosphatase, and other membrane proteins, such as prohibitin and an anion selective channel protein were identified only in the second instar, suggesting that these proteins may be involved in the higher toxicity of Cry1Ac in early instars of H. armigera. Eleven Cry1Ac binindg proteins were identified exclusively in late instar larvae, like different proteases such as trypsin-like protease, azurocidin-like proteinase, and carboxypeptidase. Different aminopeptidase N isofroms were identified in both instar larvae. We compared the Cry1Ac protoxin degradation using midgut juice from late and early instars, showing that the midgut juice from late instars is more efficient to degrade Cry1Ac protoxin than that of early instars, suggesting that increased proteolytic activity on the toxin could also explain the low Cry1Ac toxicity in late instars. 650 $aPraga de Planta 650 $aProteína 650 $aToxina 700 1 $aGOMÉZ, I. 700 1 $aSÁNCHEZ, J. 700 1 $aCASTRO, D. L. M. de 700 1 $aVALICENTE, F. H. 700 1 $aSOBERÓN, M. 700 1 $aPOLANCZYK, R. A. 700 1 $aBRAVO, A. 773 $tPlos One, San Francisco$gv. 13, n. 12, e0207789, 2018.
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