933 resultados para peroxidase enzyme
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The properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of substances on the enzyme activity, enzyme kinetics, and cyclodextrin production were analysed. Cyclodextrin glycosyltransferase was purified up to 320.74-fold by affinity chromatography using beta-cyclodextrin as the binder and it exhibited 8.71% activity recovery. This enzyme is a monomer with a molecular weight of 81.27 kDa, as estimated by SDS-PAGE. Optimum temperature and pH for cydodextrin glycosyltransferase were 55 degrees C and 8.0, respectively. The Michaelis-Menten constant was 8.62 g/l during maximum velocity of 0.858 g/l.h.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Pós-graduação em Fisiopatologia em Clínica Médica - FMB
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Pós-graduação em Agronomia (Produção Vegetal) - FCAV
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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 Ciência e Tecnologia Animal - FEIS
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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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.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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The objective of this work was to study the intercropping of Brachiaria brizantha. Marandu with soybeans. The experiment has been planted in a 3 year prevailing area with no-tillage, in eutrophic Oxisol at Maripa - PR. The experimental design was a randomized block with five replications. For the forage study, four treatments were performed which consisted of seeding times brachiaria [early ( seven days before planting soybeans) joint (same day of soybean planting) and after (at stages V-3 and R-1 culture)] intercropping with soybean. To study the yield and crude protein and oil levels of the grain were adopted six treatments, which consisted of sowing dates of capim Marandu [early (seven days before planting soybeans), joint (same day of soybean planting) after (V-3, R-1 and R-5 soybean) and in single culture (single)]. The forager higher productivity of dry matter occurs with early sowing, however, the greatest reduction in soybean yield also occurs in this case. The sowing of Brachiaria until R-5 soy has no influence on the nutritional value of the forage. The intercropped of soybean with Brachiaria brizantha. Marandu has no impact on the leaf Nitrogen content, oil content and enzyme activity of soybean peroxidase. The highest yield of soybeans occurs when it is grown single or Brachiaria is sown in stage R-5. The crude protein content of soybean grain is reduced when brachiaria seeding is early or together with soybeans compared to single culture.
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A caracterização e isolamento do gene com expressão específica em raiz de café (Coffea arabica) que codifica uma peroxidase (CaPOX) e suas respectivas regiões promotoras, permitiu realizar a caracterização da expressão desse gene em reposta a estresse biótico (infecção por nematóides) assim como a análise funcional do seu promotor. Promotores tecido-específicos responsáveis pela regulação de genes responsivos a estresses bióticos tornam-se fundamentais em programas biotecnológicos que visam o aumento da resistência e tolerância vegetal. Partindo desse princípio, realizou-se a quantificação da expressão relativa do gene CaPOX em raízes de café utilizando plantas de Coffea arabica de um cultivar susceptível (Mundo Novo) e de outro cultivar resistente (IAC 388-17-1) a nematóides, respectivamente. Em paralelo utilizou- se plantas transgênicas de tabaco (Nicotiana tabacum SR1) contendo a versão completa do promotor do gene CaPOX em fusão transcricional ao gene repórter uidA (que codifica a β-glucuronidase; GUS) . A partir disso, pode-se observar que o gene CaPOX tem sua expressão aumentada em resposta a infecção por nematóides, sendo que a indução observada ocorre nos tempos iniciais pós-inoculação. Da mesma maneira, o promotor do gene CaPOX é responsivo a infecção por nematóides, sendo ativado nos tempos iniciais pós-inoculação
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)