184 resultados para biochemical taxonomy


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Dentre as numerosas terapias para minimizar as complicações diabéticas, os antioxidantes e flavonoides são testados na clínica médica. Foi analisado o efeito da naringerina sobre os parâmetros bioquímicos em ratos diabéticos induzidos por estreptozotocina (STZ - 60mg/kg, i.p.). Ratos machos foram divididos em 4 grupos: G1: controle não tratado; G2: ratos normais que receberam naringerina; G3: diabéticos não tratados; G4: ratos diabéticos que receberam naringerina. Naringerina (50mg/kg, i.p.), decresceu a hiperglicemia e a hiperlipidemia em ratos diabéticos. A concentração sérica de insulina em ratos tratados tendeu aumentar. A naringerina preveniu as alterações, provocadas pela estreptozotocina, na atividade hepática e cardíaca de ALT, AST e LDH, indicando o efeito protetor da naringerina sobre estes tecidos, contra toxicidade provocada pela STZ. O nível de glicogênio nos tecidos cardíaco e hepático elevou com a naringerina em ratos diabéticos. A naringerina melhorou o metabolismo da glicose e de lipídios e preveniu as complicações diabéticas.

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Biochemical studies revealed that the activity of some hydrolytic enzymes from the venom glands of honey bee Apis mellifera was higher in workers of 14 days of age than in those of 40 days. Among these enzymes, the highest activity was recorded for acid phosphatase, which was cytochemically detected throughout the length of the secretory filament and surrounding the canaliculi of the distal region of the reservoir. The acid phosphatase was considered to be a typical secretion product, since it was present in the cytoplasm as well as in the canaliculi of the secretory cells. (c) 2009 Elsevier Ltd. All rights reserved.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Trigona hypogea, T. crassipes, and T. necrophaga are obligate necrophagous bees that differ from the majority of bees by using animal material instead of pollen as a protein resource. Since T. hypogea does not store protein in cerumen pots, it was thought that glandular secretions were its only larval protein source. This is in contrast to T. necrophaga which stores a yellowish proteinaceous jelly in the pots. Our results show that the larval food of T. hypogea has a higher protein content than the food stored in the pots and that it presents an electrophoretical protein pattern similar to that of the hypopharyngeal gland, indicating that workers add glandular secretions to the larval food while provisioning the brood cells. Thus, it can be suggested that T. hypogea has a provisioning behavior similar to other Meliponinae. The presence of several bands of proteins in the food stored in the pots shows that this species stores carrion mixed with honey in storage pots. Morphological data suggest that both larvae and adults make use of the same foodstuffs. These results also suggest that T. hypogea is more similar to other necrophagous species than it is to T. necrophaga (a more specialized bee).

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Aims of the study. - The aim of this study is to investigate the behavior of the physiological, biochemical and psychological parameters in Brazilian soccer players during a training program.Materials. - Fifteen athletes were evaluated at the beginning (T1), in the middle (T2) and at the end (T3) of the training program. on the first day, at 7:30 am, before the blood collecting at rest for the determination of serum creatine kinase (CK), serum creatinine and serum urea, the athletes had their psychological parameters assessed by the profile of mood state questionnaire (POMS). After 90 min, they performed a 250-m sprint. on the second day at 8:30 am, the athletes had their alactic anaerobic performance measured and, after 40 min, they completed the aerobic test. Friedman test was used to verify the behavior of overtraining markers.Results. - There was a decrease in vigor score in T3 (p=0.01) compared with T1 and T2. In T3 (p=0.01), the athletes also showed an increase in serum creatinine levels compared to T1. Furthermore, in the same period, we verified a diminishing in the team performance.Conclusion. - The training program developed between T2 and T3 led to the fall of the vigor score, the increase in serum creatinine concentrations and the diminishing in team performance. (c) 2007 Elsevier Masson SAS. All rights reserved.

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Objective To investigate the relationship between skipping meals and biochemical variables in obese children and adolescents.Study design The sample was composed of 174 obese children and adolescents, aged between 6 and 16 years (80 male and 94 female). Body composition was assessed by dual-energy x-ray absorptiometry, fasting blood glucose, and lipid profile were measured after 12 hours fasting. The frequency of skipping breakfast, lunch, or dinner was assessed through a face-to-face interview carried out with the parents.Results The prevalence of eating breakfast daily was low in boys (47.5%) and girls (44.7%). A higher frequency of eating breakfast was negatively correlated with glucose (r = -0.16; P = .026), triglycerides (r = -0.19; P = .011), and very low density lipoprotein cholesterol (r = -0.21; P = .005). In the multivariate model, the weekly frequency of eating breakfast remained negatively associated with glucose (beta = -0.975; P = .017), triglycerides (beta = -7.792; P = .017), and very low density lipoprotein cholesterol (beta = -1.870; P = .009) independent of age, sex, trunk fatness, and parents' education.Conclusion Skipping meals, mainly breakfast, is associated with glucose and lipid levels in obese children and adolescents. (J Pediatr 2012;161:871-4).

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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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Miliin, a new thiol-dependent serine protease purified from the latex of Euphorbia milii possesses a molecular weight of 79 kDa, an isoelectric point of 4.3 and is optimally active at 60 degrees C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease.

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