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 | Acesso ao texto completo restrito à biblioteca da Embrapa Amazônia Ocidental. Para informações adicionais entre em contato com cpaa.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Amazônia Ocidental. |
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Data corrente: |
10/01/2024 |
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Data da última atualização: |
19/01/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
OLIVEIRA, E. S. C.; PONTES, F. L. D.; ACHO, L. D. R.; SILVA, B. J. P. da; ROSÁRIO, A. S. do; CHAVES, F. C. M.; CAMPOS, F. R.; BEZERRA, J. de A.; LIMA, E. S.; MACHADO, M. B. |
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Afiliação: |
EDINILZE S. C. OLIVEIRA, UNIVERSIDADE FEDERAL DO AMAZONAS; FLÁVIA L. D. PONTES, UNIVERSIDADE FEDERAL DO PARANÁ; LEONARD D. R. ACHO, UNIVERSIDADE FEDERAL DO AMAZONAS; BÁRBARA JANAÍNA P. DA SILVA, UNIVERSIDADE FEDERAL DO AMAZONAS; ALESSANDRO S. DO ROSÁRIO, MUSEU PARAENSE EMILIO GOELDI; FRANCISCO CELIO MAIA CHAVES, CPAA; FRANCINETE R. CAMPOS, UNIVERSIDADE FEDERAL DO AMAZONAS; JAQUELINE DE A. BEZERRA, UNIVERSIDADE FEDERAL DO AMAZONAS; EMERSON S. LIMA, UNIVERSIDADE FEDERAL DO AMAZONAS; MARCOS B. MACHADO, UNIVERSIDADE FEDERAL DO AMAZONAS. |
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Título: |
NMR and multivariate methods: identification of chemical markers in extracts of pedra-ume-caá and their antiglycation, antioxidant, and enzymatic inhibition activities. |
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Ano de publicação: |
2024 |
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Fonte/Imprenta: |
Phytochemical Analysis, p. 1-15, 2024. |
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DOI: |
10.1002/pca.3312 |
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Idioma: |
Inglês |
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Notas: |
Online first. |
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Conteúdo: |
In Brazil, the plant group popularly known as "pedra-ume-caá" is used in folk medicine for the treatment of diabetes, and its raw material is commonly sold. The aim of the study was to apply a method for chemical identification of extracts of dry pedra-ume-caá leaves using HPLC–high-resolution mass spectrometry (HRMS) and NMR and develop a multivariate model with NMR data to authenticate commercial samples. In addition, to evaluate the biological activities of the extracts. |
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Palavras-Chave: |
Anti-AGE; Chemical markers. |
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Thesagro: |
Myrtaceae. |
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Thesaurus Nal: |
Chemometrics. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 01412naa a2200301 a 4500
001 2160642
005 2024-01-19
008 2024 bl uuuu u00u1 u #d
024 7 $a10.1002/pca.3312$2DOI
100 1 $aOLIVEIRA, E. S. C.
245 $aNMR and multivariate methods$bidentification of chemical markers in extracts of pedra-ume-caá and their antiglycation, antioxidant, and enzymatic inhibition activities.$h[electronic resource]
260 $c2024
500 $aOnline first.
520 $aIn Brazil, the plant group popularly known as "pedra-ume-caá" is used in folk medicine for the treatment of diabetes, and its raw material is commonly sold. The aim of the study was to apply a method for chemical identification of extracts of dry pedra-ume-caá leaves using HPLC–high-resolution mass spectrometry (HRMS) and NMR and develop a multivariate model with NMR data to authenticate commercial samples. In addition, to evaluate the biological activities of the extracts.
650 $aChemometrics
650 $aMyrtaceae
653 $aAnti-AGE
653 $aChemical markers
700 1 $aPONTES, F. L. D.
700 1 $aACHO, L. D. R.
700 1 $aSILVA, B. J. P. da
700 1 $aROSÁRIO, A. S. do
700 1 $aCHAVES, F. C. M.
700 1 $aCAMPOS, F. R.
700 1 $aBEZERRA, J. de A.
700 1 $aLIMA, E. S.
700 1 $aMACHADO, M. B.
773 $tPhytochemical Analysis, p. 1-15, 2024.
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Registro original: |
Embrapa Amazônia Ocidental (CPAA) |
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Voltar
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Registro Completo
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
23/01/2012 |
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Data da última atualização: |
24/02/2023 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 2 |
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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. |
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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. |
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Título: |
Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease. |
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Ano de publicação: |
2011 |
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Fonte/Imprenta: |
Biochimica et Biophysica Acta, v. 1814, n. 12, p. 1758-1768, Dec. 2011. |
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Idioma: |
Inglês |
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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. |
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Thesagro: |
Canavalia Ensiformis. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/183508/1/1-s2.0-S1570963911002172-main.pdf
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Marc: |
LEADER 02105naa a2200241 a 4500
001 1913253
005 2023-02-24
008 2011 bl uuuu u00u1 u #d
100 1 $aMULINARI, F.
245 $aCharacterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease.$h[electronic resource]
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.
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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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