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Registro Completo |
Biblioteca(s): |
Embrapa Algodão; Embrapa Cerrados; Embrapa Trigo. |
Data corrente: |
28/01/2008 |
Data da última atualização: |
17/06/2008 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
ALBRECHT, J. C.; VIEIRA, E. A.; SÓ e SILVA, M.; ANDRADE, J. M. V. de; SCHEEREN, P. L.; TRINDADE, M. da G.; SOARES SOBRINHO, J.; SOUSA, C. N. A. de; REIS, W. P.; RIBEIRO JÚNIOR, W. Q.; FRONZA, V.; CARGNIN, A.; YAMANAKA, C. H. |
Afiliação: |
Júlio César Albrecht, CPAC; Eduardo Alano Vieira, CPAC; Marcio Só e Silva, CNPT; José Maria Vilela de Andrade, CPAC; Pedro Luiz Scheeren, CNPT; Maria da Glória Trindade, CNPT; Joaquim Soares Sobrinho, CNPT; Cantidio Nicolau Alves de Sousa, CNPT; Wagner Pereira Reis, UFLA; Walter Quadros Ribeiro Júnior, CPAC; Vanoli Fronza, CNPSO; Adeliano Cargnin, CPAC; Celso Hideo Yamanaka. |
Título: |
Adaptabilidade e estabilidade de genótipos de trigo irrigado no Cerrado do Brasil Central. |
Ano de publicação: |
2007 |
Fonte/Imprenta: |
Pesquisa Agropecuária Brasileira, Brasília, v. 42, n. 12, p. 1727-1734, dez. 2007. |
Idioma: |
Português |
Palavras-Chave: |
Genotype x environment interaction; interação genótipo x ambiente; melhoramento genético; recomendação de cultivares; Varieties recommendation. |
Thesagro: |
Trigo; Triticum Aestivum. |
Thesaurus Nal: |
genetic improvement. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/CNPT-2010/9914/1/42n12a09.pdf
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Marc: |
LEADER 01092naa a2200349 a 4500 001 1559151 005 2008-06-17 008 2007 bl uuuu u00u1 u #d 100 1 $aALBRECHT, J. C. 245 $aAdaptabilidade e estabilidade de genótipos de trigo irrigado no Cerrado do Brasil Central. 260 $c2007 650 $agenetic improvement 650 $aTrigo 650 $aTriticum Aestivum 653 $aGenotype x environment interaction 653 $ainteração genótipo x ambiente 653 $amelhoramento genético 653 $arecomendação de cultivares 653 $aVarieties recommendation 700 1 $aVIEIRA, E. A. 700 1 $aSÓ e SILVA, M. 700 1 $aANDRADE, J. M. V. de 700 1 $aSCHEEREN, P. L. 700 1 $aTRINDADE, M. da G. 700 1 $aSOARES SOBRINHO, J. 700 1 $aSOUSA, C. N. A. de 700 1 $aREIS, W. P. 700 1 $aRIBEIRO JÚNIOR, W. Q. 700 1 $aFRONZA, V. 700 1 $aCARGNIN, A. 700 1 $aYAMANAKA, C. H. 773 $tPesquisa Agropecuária Brasileira, Brasília$gv. 42, n. 12, p. 1727-1734, dez. 2007.
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Registro original: |
Embrapa Cerrados (CPAC) |
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Registro Completo
Biblioteca(s): |
Embrapa Agricultura Digital. |
Data corrente: |
22/12/2015 |
Data da última atualização: |
22/12/2015 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 1 |
Autoria: |
CAMPEIRO, J. D'A.; NESHICH, I. P.; SANT'ANNA, O. A.; LOPES, R.; IANZER, D.; ASSAKURA, M. T.; NESHICH, G.; HAYASHI, M. A. F. |
Afiliação: |
JOANA D'ARC CAMPEIRO, Unifesp; IZABELLA P. NESHICH, CNPTIA; OSVALDO A. SANT'ANNA, Instituto Butantan; ROBSON LOPES, Instituto Butantan; DANIELLE IANZER, Instituto Butantan; MARINA T. ASSAKURA, Instituto Butantan; GORAN NESHICH, CNPTIA; MIRIAN A. F. HAYASHI, Unifesp. |
Título: |
Identification of snake bradykinin-potentiating peptides (BPPs)-simile sequences in rat brain: potential BPP-like precursor protein? |
Ano de publicação: |
2015 |
Fonte/Imprenta: |
Biochemical Pharmacology, New York, v. 96, n. 3, p. 202-215, Aug. 2015. |
DOI: |
http://dx.doi.org/10.1016/j.bcp.2015.05.012 |
Idioma: |
Inglês |
Conteúdo: |
Bradykinin-potentiating peptides (BPPs) from the South American pit viper snake venom were the first natural inhibitors of the human angiotensin I-converting enzyme (ACE) described. The pioneer characterization of the BPPs precursor from the snake venom glands by our group showed for the first time the presence of the C-type natriuretic peptide (CNP) in this same viper precursor protein. The confirmation of the BPP/CNP expression in snake brain regions correlated with neuroendocrine functions stimulated us to pursue the physiological correlates of these vasoactive peptides in mammals. Notably, several snake toxins were shown to have endogenous physiological correlates in mammals. In the present work, we expressed in bacteria the BPPs domain of the snake venom gland precursor protein, and this purified recombinant protein was used to raise specific polyclonal anti-BPPs antibodies. The correspondent single protein band immune-recognized in adult rat brain cytosol was isolated by 2DSDS/PAGE and/or HPLC, before characterization by MS fingerprint analysis, which identified this protein as superoxide dismutase (SOD, EC 1.15.1.1), a classically known enzyme with antioxidant activity and important roles in the blood pressure modulation. In silico analysis showed the exposition of the BPP-like peptide sequences on the surface of the 3D structure of rat SOD. These peptides were chemically synthesized to show the BPP-like biological activities in ex vivo and in vivo pharmacological bioassays. Taken together, our data suggest that SOD protein have the potential to be a source for putative BPP-like bioactive peptides, which once released may contribute to the blood pressure control in mammals. MenosBradykinin-potentiating peptides (BPPs) from the South American pit viper snake venom were the first natural inhibitors of the human angiotensin I-converting enzyme (ACE) described. The pioneer characterization of the BPPs precursor from the snake venom glands by our group showed for the first time the presence of the C-type natriuretic peptide (CNP) in this same viper precursor protein. The confirmation of the BPP/CNP expression in snake brain regions correlated with neuroendocrine functions stimulated us to pursue the physiological correlates of these vasoactive peptides in mammals. Notably, several snake toxins were shown to have endogenous physiological correlates in mammals. In the present work, we expressed in bacteria the BPPs domain of the snake venom gland precursor protein, and this purified recombinant protein was used to raise specific polyclonal anti-BPPs antibodies. The correspondent single protein band immune-recognized in adult rat brain cytosol was isolated by 2DSDS/PAGE and/or HPLC, before characterization by MS fingerprint analysis, which identified this protein as superoxide dismutase (SOD, EC 1.15.1.1), a classically known enzyme with antioxidant activity and important roles in the blood pressure modulation. In silico analysis showed the exposition of the BPP-like peptide sequences on the surface of the 3D structure of rat SOD. These peptides were chemically synthesized to show the BPP-like biological activities in ex vivo and in vivo pharmacological bio... Mostrar Tudo |
Palavras-Chave: |
Bioinformática; Endogenous correlate; Immunorecognition; Peptídeos; Pressão sanguínea; Snake toxin. |
Thesagro: |
Veneno. |
Thesaurus NAL: |
Bioinformatics; Blood pressure; Peptides. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/136051/1/Identification-snake-Campeiro.pdf
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Marc: |
LEADER 02743naa a2200337 a 4500 001 2032223 005 2015-12-22 008 2015 bl uuuu u00u1 u #d 024 7 $ahttp://dx.doi.org/10.1016/j.bcp.2015.05.012$2DOI 100 1 $aCAMPEIRO, J. D'A. 245 $aIdentification of snake bradykinin-potentiating peptides (BPPs)-simile sequences in rat brain$bpotential BPP-like precursor protein?$h[electronic resource] 260 $c2015 520 $aBradykinin-potentiating peptides (BPPs) from the South American pit viper snake venom were the first natural inhibitors of the human angiotensin I-converting enzyme (ACE) described. The pioneer characterization of the BPPs precursor from the snake venom glands by our group showed for the first time the presence of the C-type natriuretic peptide (CNP) in this same viper precursor protein. The confirmation of the BPP/CNP expression in snake brain regions correlated with neuroendocrine functions stimulated us to pursue the physiological correlates of these vasoactive peptides in mammals. Notably, several snake toxins were shown to have endogenous physiological correlates in mammals. In the present work, we expressed in bacteria the BPPs domain of the snake venom gland precursor protein, and this purified recombinant protein was used to raise specific polyclonal anti-BPPs antibodies. The correspondent single protein band immune-recognized in adult rat brain cytosol was isolated by 2DSDS/PAGE and/or HPLC, before characterization by MS fingerprint analysis, which identified this protein as superoxide dismutase (SOD, EC 1.15.1.1), a classically known enzyme with antioxidant activity and important roles in the blood pressure modulation. In silico analysis showed the exposition of the BPP-like peptide sequences on the surface of the 3D structure of rat SOD. These peptides were chemically synthesized to show the BPP-like biological activities in ex vivo and in vivo pharmacological bioassays. Taken together, our data suggest that SOD protein have the potential to be a source for putative BPP-like bioactive peptides, which once released may contribute to the blood pressure control in mammals. 650 $aBioinformatics 650 $aBlood pressure 650 $aPeptides 650 $aVeneno 653 $aBioinformática 653 $aEndogenous correlate 653 $aImmunorecognition 653 $aPeptídeos 653 $aPressão sanguínea 653 $aSnake toxin 700 1 $aNESHICH, I. P. 700 1 $aSANT'ANNA, O. A. 700 1 $aLOPES, R. 700 1 $aIANZER, D. 700 1 $aASSAKURA, M. T. 700 1 $aNESHICH, G. 700 1 $aHAYASHI, M. A. F. 773 $tBiochemical Pharmacology, New York$gv. 96, n. 3, p. 202-215, Aug. 2015.
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