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Registro Completo |
Biblioteca(s): |
Embrapa Clima Temperado. |
Data corrente: |
16/01/2015 |
Data da última atualização: |
16/01/2015 |
Tipo da produção científica: |
Artigo em Anais de Congresso |
Autoria: |
ROMMEL, R.; SEITER, R.; TATTO, F. R.; EICHOLZ, M.; EICHOLZ, E. D. |
Afiliação: |
Ruan Rommel, UNOPAR; Rudmar Seiter, UFPEL; Francis Radael Tatto, UFPEL; Marcel Eicholz, UFPEL; EBERSON DIEDRICH EICHOLZ, CPACT. |
Título: |
Arranjo de plantas para cultivar BRS energia. |
Ano de publicação: |
2014 |
Fonte/Imprenta: |
In: SIMPÓSIO ESTADUAL DE AGROENERGIA; REUNIÃO TÉCNICA DE AGROENERGIA - RS, 5.; ENCONTRO DE ENERGIAS RENOVÁVEIS NA AGRICULTURA FAMILIAR, 2., Pelotas, 2014. Anais... Pelotas: Embrapa Clima Temperado, 2014. 1 pen card. |
Idioma: |
Português |
Thesagro: |
Energia. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/115702/1/058.pdf
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Marc: |
LEADER 00615nam a2200157 a 4500 001 2005796 005 2015-01-16 008 2014 bl uuuu u00u1 u #d 100 1 $aROMMEL, R. 245 $aArranjo de plantas para cultivar BRS energia.$h[electronic resource] 260 $aIn: SIMPÓSIO ESTADUAL DE AGROENERGIA; REUNIÃO TÉCNICA DE AGROENERGIA - RS, 5.; ENCONTRO DE ENERGIAS RENOVÁVEIS NA AGRICULTURA FAMILIAR, 2., Pelotas, 2014. Anais... Pelotas: Embrapa Clima Temperado, 2014. 1 pen card.$c2014 650 $aEnergia 700 1 $aSEITER, R. 700 1 $aTATTO, F. R. 700 1 $aEICHOLZ, M. 700 1 $aEICHOLZ, E. D.
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Embrapa Clima Temperado (CPACT) |
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Registro Completo
Biblioteca(s): |
Embrapa Milho e Sorgo. |
Data corrente: |
14/11/1997 |
Data da última atualização: |
11/06/2018 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
FONTES, E. P. B.; SILVA, C. J.; CAROLINO, S. M. B.; FIGUEREDO, J. D. F.; BATISTA, D. P. O. |
Afiliação: |
EMBRAPA/CNPMS. |
Título: |
A soybean binding protein (BiP) homolog is temporally regulated in soybean seeds and associates detectably with normal storage proteins in vitro. |
Ano de publicação: |
1996 |
Fonte/Imprenta: |
Brazilian Journal of Genetics, Ribeirão Preto, v. 19, n. 2, p. 305-312, 1996. |
Idioma: |
Inglês |
Conteúdo: |
The endoplasmic reticulum (ER) luminal binding protein (BiP) is thought to be a key mediator of folding and assembly of de novo synthesized secretory proteins. We have used a maize (Zea mays L.) BiP antibady to identify its homolog in soybeans (Glycine max (L.) Merril). The accumulation of BiP in developing soybean seeds seems to be coordinated with the onset of active storage protein synthesis. We used a co-immunoprecipitation assay to detect soybean BiP:B-conglycinin interactions. Either a maize BiP antibody or a-B-conglycinin antibody co-immunoprecipitated the reciprocal protein from whole seed protein extract enzymatically depleted of adenosine 5-triphosphate (ATP), while an unrelated antibody failed to immunoprecipitate either one. The association ofBiP:B-conglycinin complexes was completely reversed by addition of ATP, a diagnostic feature of molecular chaperone-mediated interaction. However, only a very small fraction of B-conglycinin was found to be associated with BiP in whole cell protein extracts from immature seeds. These results are consistent with a transient association between BiP and B-conglycinin subunits, and suggests its involvement in the biosynthetic transport pathway of storage proteins to protein bodies. |
Palavras-Chave: |
Protein; Seed; Soybean. |
Thesagro: |
Biologia Molecular; Glycine Max; Proteína; Semente; Soja. |
Thesaurus NAL: |
molecular biology. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/38228/1/Soybean-binding.pdf
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Marc: |
LEADER 02091naa a2200277 a 4500 001 1477302 005 2018-06-11 008 1996 bl uuuu u00u1 u #d 100 1 $aFONTES, E. P. B. 245 $aA soybean binding protein (BiP) homolog is temporally regulated in soybean seeds and associates detectably with normal storage proteins in vitro.$h[electronic resource] 260 $c1996 520 $aThe endoplasmic reticulum (ER) luminal binding protein (BiP) is thought to be a key mediator of folding and assembly of de novo synthesized secretory proteins. We have used a maize (Zea mays L.) BiP antibady to identify its homolog in soybeans (Glycine max (L.) Merril). The accumulation of BiP in developing soybean seeds seems to be coordinated with the onset of active storage protein synthesis. We used a co-immunoprecipitation assay to detect soybean BiP:B-conglycinin interactions. Either a maize BiP antibody or a-B-conglycinin antibody co-immunoprecipitated the reciprocal protein from whole seed protein extract enzymatically depleted of adenosine 5-triphosphate (ATP), while an unrelated antibody failed to immunoprecipitate either one. The association ofBiP:B-conglycinin complexes was completely reversed by addition of ATP, a diagnostic feature of molecular chaperone-mediated interaction. However, only a very small fraction of B-conglycinin was found to be associated with BiP in whole cell protein extracts from immature seeds. These results are consistent with a transient association between BiP and B-conglycinin subunits, and suggests its involvement in the biosynthetic transport pathway of storage proteins to protein bodies. 650 $amolecular biology 650 $aBiologia Molecular 650 $aGlycine Max 650 $aProteína 650 $aSemente 650 $aSoja 653 $aProtein 653 $aSeed 653 $aSoybean 700 1 $aSILVA, C. J. 700 1 $aCAROLINO, S. M. B. 700 1 $aFIGUEREDO, J. D. F. 700 1 $aBATISTA, D. P. O. 773 $tBrazilian Journal of Genetics, Ribeirão Preto$gv. 19, n. 2, p. 305-312, 1996.
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Embrapa Milho e Sorgo (CNPMS) |
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