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The satisfaction of university students with the variables that regulate their learning provides very valuable information to improve the quality of teaching processes. The main objective of this study was to evaluate the learning of Brazilian university students, exploring both self-regulation variables, such as study techniques; and more external regulation variables, namely, satisfaction with the teaching-learning process and with the infrastructure, based on three variables: gender, the institution of higher education and the academic year of the students. To achieve this, 560 students of the Pedagogy degree were evaluated with two questionnaires: a questionnaire of satisfaction with the educational infrastructure and the teaching-learning process and a questionnaire on study techniques. Statistically significant differences were obtained, especially depending on the type of institution and the academic year. The students of private schools and earlier academic years were the ones who obtained the most satisfaction with the study techniques and with the infrastructure. Those from private centers also expressed more satisfaction with the teaching-learning processes. These results provide greater knowledge about the processes of self-regulation and external regulation of university learning and of their satisfaction with them, which can contribute to improving educational policies in Brazil.

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En este estudio se evaluó la eficacia de la hipnosis en la modificación de un conjunto de variables psicológicas y fisiológicas durante la realización de pruebas de esfuerzo. Se utilizaron un total de 24 participantes ciclistas. El procedimiento consistió en enviar al azar a los participantes a un grupo experimental con hipnosis o al grupo control. En ambos grupos se midieron variables psicológicas y fisiológicas relacionadas con el deporte. Los resultados no mostraron diferencias estadísticamente significativas entre-grupos en las variables evaluadas. Sí se observó una tendencia en el grupo experimental a puntuar más positivamente en varias variables psicológicas analizadas. Se concluye que sería de interés desarrollar futuras investigaciones ampliando el tamaño de la muestra y aplicar el procedimiento en diferentes modalidades deportivas.

In this paper evaluated the efficiency of hypnosis on modification of a set of psychological and physiological variables during the performance of a task force. There were in use a total of 24 cycle participants. The procedure consisted of sending at random to the participants to an experimental group with hypnosis and group control. In both groups there measured up psychological and physiological variables related to the sport. Results indicate that there was not a statistically significant difference between the two groups. However, a tendency more positively in a set of psychological variables was observed in the experimental group. It is concluded that it would be of interest to develop future researches extending the size of the sample and to apply the procedure in different sports modalities.

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Soybean fields provide habitats for many species of amphibians. However, the persistence and health of amphibian populations may be at risk from the increasing use of pesticides and other agricultural chemicals. We examined the activities of acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and carboxylesterases (CbEs) in 11 syntopic species of larval anurans. In vitro effects of malaoxon causing 50% BChE inhibition (IC(50)) were also studied. In addition, we calculated a relative risk index (RI) based on the geographic distributions of the anurans, the phenology of soybean cultivation, and basal enzymatic values related to potential pesticide detoxification. Among the 11 species, AChE activity varied from 17.5 ± 1.6 to 68.2 ± 4.7 nmol min(-1) mg(-1) protein (PT). BChE activity also varied significantly, ranging from 3.3 ± 0.4 to 7.5 ± 0.4 nmol min(-1) mg(-1)PT. Both measures of CbE activities varied widely (CbE α-NA: 2.1 ± 0.5-12.4 ± 1.1 nmol min(-1) mg(-1) PT; CbE-4NPV: 21.8 ± 1.8-102.6 ± 7.9 nmol min(-1) mg(-1) PT). We also corroborate that lower BChE activity levels for the tadpoles were associated at minor IC(50) values. The results of this study demonstrate significant variation in enzymatic levels among several tadpole species and intermediate to high RI values for 7 species. Based on these results, it appears that a conversion of native ecosystems to soybean crops may lead to increased ecological risk for anuran amphibians.

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Alpha 1,2-mannosidases from glycosyl hydrolase family 47 participate in N-glycan biosynthesis. In filamentous fungi and mammalian cells, alpha1,2-mannosidases are present in the endoplasmic reticulum (ER) and Golgi complex and are required to generate complex N-glycans. However, lower eukaryotes such Saccharomyces cerevisiae contain only one alpha1,2-mannosidase in the lumen of the ER and synthesise high-mannose N-glycans. Little is known about the N-glycan structure and the enzyme machinery involved in the synthesis of these oligosaccharides in the dimorphic fungus Sporothrix schenckii. Here, a membrane-bound alpha-mannosidase from S. schenckii was solubilised using a high-temperature procedure and purified by conventional methods of protein isolation. Analytical zymograms revealed a polypeptide of 75 kDa to be responsible for enzyme activity and this purified protein was recognised by anti-alpha1,2-mannosidase antibodies. The enzyme hydrolysed Man(9)GlcNAc(2) into Man(8)GlcNAc(2) isomer B and was inhibited preferentially by 1-deoxymannojirimycin. This alpha1,2-mannosidase was localised in the ER, with the catalytic domain within the lumen of this compartment. These properties are consistent with an ER-localised alpha1,2-mannosidase of glycosyl hydrolase family 47. Our results also suggested that in contrast to other filamentous fungi, S. schenckii lacks Golgi alpha1,2-mannosidases and therefore, the processing of N-glycans by alpha1,2-mannosidases is similar to that present in lower eukaryotes.

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RESUMO

Alpha 1,2-mannosidases from glycosyl hydrolase family 47 participate in N-glycan biosynthesis. In filamentous fungi and mammalian cells, á1,2-mannosidases are present in the endoplasmic reticulum (ER) and Golgi complex and are required to generate complex N-glycans. However, lower eukaryotes such Saccharomyces cerevisiae contain only one á1,2-mannosidase in the lumen of the ER and synthesise high-mannose N-glycans. Little is known about the N-glycan structure and the enzyme machinery involved in the synthesis of these oligosaccharides in the dimorphic fungus Sporothrix schenckii. Here, a membrane-bound á-mannosidase from S. schenckii was solubilised using a high-temperature procedure and purified by conventional methods of protein isolation. Analytical zymograms revealed a polypeptide of 75 kDa to be responsible for enzyme activity and this purified protein was recognised by anti-á1,2-mannosidase antibodies. The enzyme hydrolysed Man9GlcNAc2 into Man8GlcNAc2 isomer B and was inhibited preferentially by 1-deoxymannojirimycin. This á1,2-mannosidase was localised in the ER, with the catalytic domain within the lumen of this compartment. These properties are consistent with an ER-localised á1,2-mannosidase of glycosyl hydrolase family 47. Our results also suggested that in contrast to other filamentous fungi, S. schenckii lacks Golgi á1,2-mannosidases and therefore, the processing of N-glycans by á1,2-mannosidases is similar to that present in lower eukaryotes.

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