987 resultados para Lipase EC 3.1.1.3
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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The work aimed to study the formation of Tabebuia chrysotricha Standi, seedlings in function of four substrates, varying the covering fertilization solutions. To compose the substrate it was used fibrous and granulated coconut fiber obtaining the following treatments: 100% fibrous (100% F), 60% fibrous + 40% granulated (60% F+40% G), 40% fibrous + 60% granulated (40% F+60% G) and 100% granulated (100% G). The basis fertilization was the same for all treatments and the solutions of covering fertilization varied in order to obtain complete solutions with electric conductivities of 1.06 dS m-1, 2.12 dS m-1, 3.2 dS m-1 and 4.25 dS m-1. The propagative material was sowed directly in plastic containers (120mL) with the respective substrates. The fertilization was received through sub-irrigation once a week, respecting the treatments of fertilizations. Seedlings produced in 100%G had been taller and higher than the others. The chemical analyses of aerial part were obtained when the seedlings were ready for expedition (height of 20 cm). The seedlings production in substrate 100% F and 60% F+40% G allowed them to have higher N, S, B, Mn and Zn concentrations in the aerial part. The production of T. chrysotricha seedlings is recommended in granulated coconut fiber substrate and fertilizer solutions with EC of 1.06 dS m-1.
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Pós-graduação em Biotecnologia - IQ
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Pós-graduação em Biotecnologia - IQ
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Pós-graduação em Biotecnologia - IQ
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Endo-oligopeptidase A, EC 3.4.22.19, converts small enkephalin-containing peptides into the corresponding enkephalins in vitro. We investigated the presence of endooligopeptidase A in the retina and its possible colocalization with enkephalins in retinal neurons. The specific activity of endo-oligopeptidase A found in pigeon retinae (30.3 +/- 7.3 mU/mg, mean +/- standard deviation) was four times higher than in rabbit retinae (7.0 +/- 1.1 mU/mg). The enzyme activity was not modified by EDTA, but it was enhanced by dithiothreitol and inhibited by zinc and 5,5'-dithiobis(2-nitrobenzoic acid). Immunohistochemical experiments with a purified antiserum against rabbit endo-oligopeptidase A revealed labeled neurons in both the inner nuclear layer and the ganglion cell layer of pigeon and rabbit retinae. Double-labeling immunofluorescence experiments demonstrated that about 90% of neurons containing endo-oligopeptidase A-like immunoreactivity also contained [Leu5]-enkephalin-like immunoreactivity. These colocalization results may represent an important step toward the demonstration of the possible involvement of endo-oligopeptidase A in enkephalin generation in vivo.