1000 resultados para Proteínas de Transporte


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The kinetic of jejunal glucose transport was studied using perfused rat jejunum in vivo. Ninety rats were fed a diet deficient in niacin and 90 a control diet. The jejunal loops of 7 groups of animal were infused each group with one of following solutions of glucose: 5, 10, 20, 40, 80, 160 and 300 mM/l. The Vmax and Km values were determined. The results showed that the vitamin-deficient rats absorbed less glucose independently of the amount infused and these animals had lower Vmax (133.7 microM/15 min/15 cm) and Km (192.1 mM/l) than control groups (294.1 microM/15 min/15 cm and 171.8 mM/l, respectively). In conclusion one can assume that niacin deficiency leads to a decreased glucose absorption in the jejunal loops, when tested as in our experimental model.

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The active electrogenic absorption of glucose was studied in 12 niacin deficient rats using a method for measuring changes in transmural potential difference across jejunal mucosa. The glucose was infused in 6 different concentrations (2.5; 5.0; 10.0; 20.0; 50.0 and 100.0 mM/L) at a constant rate of 1.7 ml per minute. The apparent kinetic parameters (Km and Pdmax) of active electrogenic transport were obtained graphically from curves of glucose transfer potentials. The results were compared with that obtained in a control group. The curve of glucose transfer potential in niacin deficient group was significantly lower than that of the control group. The apparent Km of niacin deficient group was greater than in the control group (16.1 x 12.7 mM/L). Furthermore, the Pdmax of the deficient group was lower than that of the control group (12.5 x 19.4 mV). The results showed that in niacin deficiency occurs a decreasing of the active electrogenic glucose absorption. One of the possible interpretation of the differences in the kinetic characteristics of electrogenic glucose transport would be a depleted energy supplement for the active transport in the enterocyte of the niacin deficient rats.

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The experiment with pheasants in initial growth phase (1 to 35 days of age), which had as its objective evaluating the nutritional needs of pheasants in the growth phase as to protein levels in the diets, was conducted on a pheasant farm located at Ribeirão Preto, SP, Brazil. Small pheasants were used, which were submitted to isocaloric diets containing 26%, 28% and 30% of crude protein. The experimental design was totally random with four repetitions of 30 birds per parcel, totaling 360 birds. The results showed that a 30% crude protein level should be recommended for pheasants in the growth phase (1 to 35 days of age).

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This review aims to report the major control mechanisms of protein and peptides digestion of special interest in human patients. Regarding protein assimilation its digestive process begins at the stomach with some not so indispensable actions comparatively to those of duodenal/jejunal lumen. However even the intestine processes are partially under gastric secretion control. Proteolytic enzyme activities are related to protein structure and amino acid constituents, tertiary and quartenary structures need HCl - denaturation prior to enzymatic hydrolysis. Thereafter the exopeptidases are guided by either NH 2 (aminopeptidases) or COOH (carboxypeptidases) terminals of the molecule while endopeptidases are oriented by the specific amino acids constituents of the peptide. Both dietary and luminal secreted proteins and polypeptides undergo to either limited or complete proteolysis resulting basic or neutral free-amino acids (40%) or dioctapeptides. The brush border peptidases continue to degrade oligopeptide to di-tripeptides and neutral free-amino acids. Some peptides are uptaked by the enterocytes whose cytosolic peptidases complete the hydrolysis. Hence the digestive products flowing in the portal vein are mainly free-amino acids from either luminal or cytosolic hydrolysis and some di-tripeptides intactly absorbed. Both mechanical and chemical processes of digestion are under neural (vagal), neuroendocrinal(acetilcholine),endocrinal(gastrin, secretin and cholecystokinin) or paracrinal (histamine) controls. The gastric phase (hydrochloric acid and pepsinogen secretions) is activated by gastrin, histamine and acetilcholine which respond to both dietary-amino acids (tryptophan and phenylalanine) and mechanic distention of stomach. The pancreatic secretion is stimulated by either cephalic or gastric phases and has influence on the intestinal phase of digestion. The intestinal types of cells S and I release secretin and cholecystokinin respectively in response of acid quimo (cells S) or amino acids and peptides (cells I) in the lumen. Secretin stimulates the releasing of water, bicarbonate and enteropeptidases whereas cholecystokinin acts on pancreatic enzymes.

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This work is aimed to determine the profile of electrophoretic serum protein in healthy adult broiler breeders (Gallus gallus domesticus) of the Avian farm strain. Fifteen breeders aging 63 weeks from Conchas, city located in the State of São Paulo, were assessed. The biuret method was used to obtain the total serum protein values and protein fractions separation through electrophoresis technique in agarose gel, and film reading through densitometry in 520nM. Seven fractions were obtained, whereas, β 1 - globulin and β 2 - globulin were not cited by the authors in the textbooks checked. The prealbumin fraction was identified only in six out of 15 samples analyzed. In five breeders, it was observed the division of g - globulin into two fractions named g - 1 and g - 2, according to the electrophoretic mobilities. The relation albumin/globulin (A/G) found in the experiment agrees with the other authors cited, demonstrating that it decreases as the age increases.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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The genus Yersinia contains three species pathogenic to humans: Y. pestis, Y. enterocolitica e Y. pseudotuberculosis. The pathogenicity of Yersinia is linked to the presence of a 70-kb virulence plasmid (pYV) that is common to the three species and codifies a type III secretion system and a set of virulence proteins, including those known as Yersinia outer proteins (Yops), that are exported by this system when the bacteria encounter host cells. Two Yops translocators (YopB and YopD) are inserted into the host plasma membrane and transport six effectors (YopO, YopH, YopM, YopJ and YopT) across the membrane into the cytosol of the host cell. The Yops effectors interfere with multiple signaling pathways of the infected cell, affecting both the innate and adaptive immune responses. This article focuses on the role of Yops in the modulation of the host immune response.

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Applying lime on the soil surface in soils managed under no-tillage has caused an excess of basic cations in the most superficial layers of the soil profile. On the other hand, subsoil acidity is considered a constraint to the development of deep plant roots. The objective of this study was to evaluate Ca 2+, Mg 2+, NO 3- and SO 4 2- leaching in the soil profile as affected by liming and top dressing nitrogen fertilization in cotton, grown with straw cover on the soil surface. Cotton plants (Gossypium hirsutum) were grown for 60 days in PVC columns filled with a Distroferric Red Latosol (sand loam Rhodic Oxisol) with liming applied over the straw on the soil surface, incorporated liming 0-20 cm deep, or without liming. Nitrogen was applied at rates of 0, 50, 100 and 150 kg ha -1 as ammonium sulfate. The PVC columns were set up in layers of 0-5, 5-10, 10-20, 20-30 and 30-30 cm, totaling 15.71 dm 3. The ammonium sulfate application caused intense leaching of SO 4 2- in the soil, irrespective of the lime application method. Liming increased the concentration of NO 3 in the 0-20 cm soil layer, whereas the correction of the soil acidity did not affect the NO 3- concentration in the 30-50 cm soil layer. The influence of ammonium sulfate on Ca 2+ leaching below 20 cm was only observed in the soil with incorporated lime. Nitrogen application resulted in extensive Mg 2+ leaching from the soil, regardless of the lime application method. In the soil layer below 30 cm, SO 4 2- presented a higher correlation than NO 3- in the formation of ionic pairs with Ca 2+ and Mg 2+.

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The effects of CO2 application through irrigation water, and of grafting in transport of 15N and in the tomato production, were studied. These treatments were arranged in a 2 x 2 factorial scheme (with and without CO2 in irrigation water and grafted and non-grafted tomato), in a completely randomized design, with four replications. The injection of CO2 into the water began at 34 days after transplant of seedlings (DAT) and continued for all irrigations. The application of the sulfate of ammonium with abundance in atoms of 15N of 3.13% in plants destined to analysis was done at 45 DAT when the plants were in the middle of fructification. After 14 days of fertilizer (15N) application the plants were harvested, washed, dried and sent for analysis of 15N in plant tissue. The results demonstrated that CO2 and the grafting did not alter the transport of 15N in the plant. The production of commercial fruits was larger when CO2 was applied in water.

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Considered as one of the main agents of the tripanossomiases, Trypanosoma evansi causes a disease generically know as surra, with wide geographic occurence. This work has the aim to study the electrophoretic profile of the acute phase proteins of goats, experimentally infected with T. evansi. Ten crossbread female goats, around 4 months of age, clinically healthy and serum negative for the presence of antibodies anti-T. evansi (IFAT) were used. The animals were divided in two groups: six were inoculated (G1) intravenously with 2,38 × 10 6 tripomastigotes of T. evansi and four were kept as noninfected controls. The blood for serum was collected daily until the 14 days after inoculation (DAI), weekly up to the 98 th DAI and every two weeks up to the 364 th DAI. The serum proteins were separacted by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDSPAGE). Twenty-one proteins were found in the serum of the goats, eight were nominally identified; phosphorylase, transferrin, albumin, antitrypsin, acid glicoprotein, haptoglobin, hemoglobin, and light chain immunoglobulin.