| |
|
|
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Hortaliças. |
|
Data corrente: |
28/11/2001 |
|
Data da última atualização: |
28/11/2001 |
|
Autoria: |
PANOBIANCO, M.; MARCOS-FILHO, J. |
|
Título: |
Comparação entre métodos para avaliação da qualidade fisiólogica de sementes de pimentão. |
|
Ano de publicação: |
1998 |
|
Fonte/Imprenta: |
Revista Brasileira de Sementes, Brasília, DF, v. 20, n. 2, p. 306-310, 1998. |
|
Idioma: |
Português |
|
Palavras-Chave: |
Physiological quality; Qualidade fisiológica; Sweet pepper; Vigour. |
|
Thesagro: |
Capsicum Annuum; Germinação; Pimentão; Semente. |
|
Thesaurus Nal: |
germination; seeds; vigor. |
|
Categoria do assunto: |
-- |
|
Marc: |
LEADER 00726naa a2200253 a 4500
001 1769536
005 2001-11-28
008 1998 bl uuuu u00u1 u #d
100 1 $aPANOBIANCO, M.
245 $aComparação entre métodos para avaliação da qualidade fisiólogica de sementes de pimentão.
260 $c1998
650 $agermination
650 $aseeds
650 $avigor
650 $aCapsicum Annuum
650 $aGerminação
650 $aPimentão
650 $aSemente
653 $aPhysiological quality
653 $aQualidade fisiológica
653 $aSweet pepper
653 $aVigour
700 1 $aMARCOS-FILHO, J.
773 $tRevista Brasileira de Sementes, Brasília, DF$gv. 20, n. 2, p. 306-310, 1998.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Hortaliças (CNPH) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
 | Acesso ao texto completo restrito à biblioteca da Embrapa Cerrados. Para informações adicionais entre em contato com cpac.biblioteca@embrapa.br. |
Registro Completo
|
Biblioteca(s): |
Embrapa Cerrados. |
|
Data corrente: |
22/12/2011 |
|
Data da última atualização: |
22/12/2011 |
|
Tipo da produção científica: |
Artigo em Periódico Indexado |
|
Circulação/Nível: |
A - 2 |
|
Autoria: |
MULINARI, F.; BECKER-RITT, A. B.; DEMARTINI, D. R.; LIGABUE-BRAUN, R.; STANISÇUASKI, F.; VERLI, H.; FRAGOSO, R. R.; SCHROEDER, E. K.; CARLINI, C. R.; GROSSI-de-SÁ, M. F. |
|
Afiliação: |
FERNANDA MULINARI, UFRGS; ARLETE BEATRIZ BECKER-RITT, UFRGS; DIOGO RIBEIRO DEMARTINI, UFRGS; RODRIGO LIGABUE-BRAUN, UFRGS; FERNANDA STANISÇUASKI, UFRGS; HUGO VERLI, UFRGS; RODRIGO DA ROCHA FRAGOSO, CPAC; EVELYN KOECHE SCHROEDER, UFRGS; CÉLIA REGINA CARLINI, UFRGS; MARIA FATIMA GROSSI DE SA, CENARGEN. |
|
Título: |
Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease. |
|
Ano de publicação: |
2011 |
|
Fonte/Imprenta: |
Biochimica et Biophysica Acta, v. 1814, n. 12, p. 1758-1768, Dec. 2011. |
|
ISSN: |
1570-9639 |
|
Idioma: |
Inglês |
|
Conteúdo: |
Ureases, nickel-dependent enzymes that catalyze the hydrolysis of urea into ammonia and bicarbonate, are
widespread in plants, bacteria, and fungi. Previously, we cloned a cDNA encoding a Canavalia ensiformis urease
isoform named JBURE-II, corresponding to a putative smaller urease protein (78 kDa) when compared to
other plant ureases. Aiming to produce the recombinant protein, we obtained jbure-IIb, with different 3? and
5? ends, encoding a 90 kDa urease. Three peptides unique to the JBURE-II/-IIb protein were detected by mass
spectrometry in seed extracts, indicating that jbure-II/-IIb is a functional gene. Comparative modeling indicates
that JBURE-IIb urease has an overall shape almost identical to C. ensiformis major urease JBURE-I with
all residues critical for urease activity. The cDNA was cloned into the pET101 vector and the recombinant protein
was produced in Escherichia coli. The JBURE-IIb protein, although enzymatically inactive presumably due
to the absence of Ni atoms in its active site, impaired the growth of a phytopathogenic fungus and showed
entomotoxic properties, inhibiting diuresis of Rhodnius prolixus isolated Malpighian tubules, in concentrations
similar to those reported for JBURE-I and canatoxin. The antifungal and entomotoxic properties of the
recombinant JBURE-IIb apourease are consistent with a protective role of ureases in plants. |
|
Thesagro: |
Canavalia Ensiformis. |
|
Categoria do assunto: |
-- |
|
Marc: |
LEADER 02108naa a2200253 a 4500
001 1910728
005 2011-12-22
008 2011 bl --- 0-- u #d
022 $a1570-9639
100 1 $aMULINARI, F.
245 $aCharacterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease.
260 $c2011
520 $aUreases, nickel-dependent enzymes that catalyze the hydrolysis of urea into ammonia and bicarbonate, are widespread in plants, bacteria, and fungi. Previously, we cloned a cDNA encoding a Canavalia ensiformis urease isoform named JBURE-II, corresponding to a putative smaller urease protein (78 kDa) when compared to other plant ureases. Aiming to produce the recombinant protein, we obtained jbure-IIb, with different 3? and 5? ends, encoding a 90 kDa urease. Three peptides unique to the JBURE-II/-IIb protein were detected by mass spectrometry in seed extracts, indicating that jbure-II/-IIb is a functional gene. Comparative modeling indicates that JBURE-IIb urease has an overall shape almost identical to C. ensiformis major urease JBURE-I with all residues critical for urease activity. The cDNA was cloned into the pET101 vector and the recombinant protein was produced in Escherichia coli. The JBURE-IIb protein, although enzymatically inactive presumably due to the absence of Ni atoms in its active site, impaired the growth of a phytopathogenic fungus and showed entomotoxic properties, inhibiting diuresis of Rhodnius prolixus isolated Malpighian tubules, in concentrations similar to those reported for JBURE-I and canatoxin. The antifungal and entomotoxic properties of the recombinant JBURE-IIb apourease are consistent with a protective role of ureases in plants.
650 $aCanavalia Ensiformis
700 1 $aBECKER-RITT, A. B.
700 1 $aDEMARTINI, D. R.
700 1 $aLIGABUE-BRAUN, R.
700 1 $aSTANISÇUASKI, F.
700 1 $aVERLI, H.
700 1 $aFRAGOSO, R. R.
700 1 $aSCHROEDER, E. K.
700 1 $aCARLINI, C. R.
700 1 $aGROSSI-de-SÁ, M. F.
773 $tBiochimica et Biophysica Acta$gv. 1814, n. 12, p. 1758-1768, Dec. 2011.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Cerrados (CPAC) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
Fechar
|
| Expressão de busca inválida. Verifique!!! |
|
|
