993 resultados para peroxidase


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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Benzidine and diamino benzidine (DAB) oxidation, typically performed by peroxidases, was demonstrated by light and electron microscopy in peroxisomes, mitochondria and membranous structures which occurred in close contact with urate crystals in Malpighian tubules of nymphs and adults of Triatoma infestans. Peroxisomes were predominantly identified in cells of the distal region of the tubules, which is engaged in excretory mechanisms. DAB oxidation in mitochondria, even in the absence of hydrogen peroxide, may indicate the existence of a mitochondrial peroxidase and possibly a cytochrome c peroxidase. The localization of the extracellular membranous structures appeared restricted to the lumen of the proximal region of the tubules and they were assumed to be remnants of endoplasmic reticulum containing peroxidases.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Objective: To evaluate the effect of periodontal therapy on clinical parameters as well as on total salivary peroxidase (TSP) activity and myeloperoxidase (MPO) activity in the gingival crevicular fluid (GCF) of patients with type 2 diabetes mellitus (DM2) and of systemically healthy individuals.Material and Methods: Twenty DM2 subjects with inadequate metabolic control (test group) and 20 systemically healthy individuals (control group), both groups with chronic periodontitis, were enrolled. Periodontal clinical parameters, namely periodontal probing depth (PD), clinical attachment level (CAL), visible plaque index (VPI), bleeding on probing (BOP), gingival bleeding index (GBI) and presence of suppuration (SUP), as well as TSP activity and GCF MPO activity, were assessed before and 3 months after non-surgical periodontal therapy.Results: At baseline and 3 months post-treatment, the test group presented a higher percentage of sites with VPI and BOP (p < 0.01). MPO activity in the GCF presented lower values (p < 0.05) for the test group at both baseline and the post-treatment period. The periodontal treatment resulted in a significant improvement of most clinical and enzymatic parameters for both groups (p < 0.05).Conclusions: In both groups, the periodontal therapy was effective in improving most clinical parameters and in reducing salivary and GCF enzymatic activity. The diabetic individuals presented lower MPO activity in the GCF.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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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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Enzimas Peroxidases são heme-proteínas encontradas nos diferentes organismos vivos, especialmente vegetais, apresentam importante papel fisiológico/bioquímico como proteção contra microorganismos invasores. A soja, um dos mais importantes produtos para o agronegócio brasileiro apresenta na casca de suas sementes (subproduto) alta atividade de peroxidase, denominada soybean peroxidase,com potencial de utilização em métodos analíticos clínicos. A proposta do trabalho foi aplicar o planejamento fatorial para otimização das condições extração da enzima, definição das condições ótimas de atividade (pH e temperatura), utilizando metodologia de superfície de resposta. Os dados obtidos com clara definição foram: i) extração em pó cetonico, ii) meio reacional: pH 3,3, volume da amostra contendo a enzima 330 µL - 340 µL, peróxido de hidrogênio 4,2 mmol.L-1 150 µL, tempo de reação 20 segundos, temperatura 50º C, substrato guaiacol 30mmol.L-1 300 µL, e 0,1 mol.L-1 de NaCl. O uso da dessa metodologia para definição das condições de extração e estudos cinético-enzimáticos da peroxidase de soja foram eficientes e mais precisos, comparado a metodologia de variações/repetições (tentativa e erro).

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A influência de estresse induzido por cloreto de sódio (75 e 150 mM) sobre o conteúdo de carboidratos solúveis e atividade da peroxidase, foi estudada em plântulas de mandioca cultivadas in vitro. Os resultados mostraram que a atividade da peroxidase diminuiu gradualmente durante o crescimento de plântulas em todos os tratamentos. O conteúdo de açúcares redutores foi menor em plântulas submetidas a 75 mM de NaCl, nas fases mais adiantadas do desenvolvimento, em comparação com a dose mais elevada do sal (150 mM de NaCl) ou sua omissão. Os resultados obtidos indicaram que o NaCl alterou o metabolismo de carboidratos, atividade da peroxidase e o crescimento de plântulas cultivadas in vitro.

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O teor de poliaminas (putrescina, espermidina e espermina) e a atividade enzimática da peroxidase (EC 1.11.1.7) foram determinados em plantas de Phaseolus vulgaris L. cv Carioquinha, após terem sido submetidas a estresse salino (50 e 100 mM de NaCl). Foram observadas alterações nos teores das poliaminas, principalmente putrescina, que aumentou com o tempo e a concentração de NaCl. Também ocorreu aumento na atividade da peroxidase em ambas concentrações de NaCl utilizadas. Os resultados mostraram alterações no metabolismo de poliaminas e peroxidases nas plantas de feijão cultivadas em meio salino.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Peroxidase from peach fruit was purified 28.9-fold by DEAE-cellulose, Sephadex G-100 and hydroxylapatite chromatography. The purified enzyme showed only one peak of activity with an optimum pH of 5.0 and temperature of 40 degreesC. The calculated activation energy (Ea) for the reaction was 7.97 kcal/mol. The enzyme was heat-labile in the temperature range of 60 to 80 degreesC with a fast inactivation at 80 degreesC. PAGE of the inactivation course at 70 degreesC showed only one band of activity. Different sugars increased the heat stability of the activity in the following order: sucrose>lactose>glucose>fructose. Measurement of residual activity showed a stabilizing effect of sucrose at various temperature/sugar concentrations (10 to 40%, w/w) with the Ea for inactivation increasing with sucrose concentration from 0 to 20% (w/w). After inactivation at 70 degreesC and 75 degreesC the enzyme was able to be reactivated by up to 40% of the initial activity when stared at 30 degreesC.

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1. In order to investigate the effect of aging on the erythrocyte glutathione system, total glutathione (GSH), glutathione reductase (GSH-red) and glutathione peroxidase (GSH-px) levels were measured in erythrocytes from 33 young (mean age = 30.5 +/- 9.7 years) and 28 aged (mean age = 68.9 +/- 11.4 years) healthy individuals.2. GSH was 3.5 +/- 1.8-mu-M/g Hb for the young group, a value significantly greater (P < 0.01) than 2.3 +/- 0.9-mu-M/g Hb found for the aged group. Similarly, GSH-red activity, 5.5 +/- 1.8 IU/g Hb, was higher (P < 0.05) for the young group than 3.4 +/- 0.9 IU/g Hb found for the aged group. The GSH-px activity levels for the young group, 21.1 +/- 5.9 IU/g Hb, were significantly greater (P < 0.01) than 12.0 +/- 3.3 IU/g Hb for the aged group. The lower activity detected in the aged group for all of these parameters of the glutathione redox system was not related to low levels of hematocrit or hemoglobin.3. There was no statistical difference in the activation coefficient (AC) of reductase (+FAD/-FAD) between groups, which seems to indicate that the lower activity of glutathione reductase observed in the aged group was not due to riboflavin deficiency.4. Additional information is required to determine the mechanisms controlling the glutathione redox system and its role in the aging process.