911 resultados para source localization


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Carbon dioxide released from alcoholic fermentation accounts for 33% of the whole CO(2) involved in the use of ethanol as fuel derived from glucose. As Arthrospira platensis can uptake this greenhouse gas, this study evaluates the use of the CO(2) released from alcoholic fermentation for the production of Arthrospira platensis. For this purpose, this cyanobacterium was cultivated in continuous process using urea as nitrogen source, either using CO(2) from alcoholic fermentation, without any treatment, or using pure CO(2) from cylinder. The experiments were carried out at 120 mu mol photons m(-2) s(-1) in tubular photobioreactor at different dilution rates (0.2 <= D <= 0.8 d(-1)). Using CO(2) from alcoholic fermentation, maximum steady-state cell concentration (2661 +/- 71 mg L(-1)) was achieved at D 0.2 d(-1), whereas higher dilution rate (0.6 d(-1)) was needed to maximize cell productivity (839 mg L(-1) d(-1)). This value was 10% lower than the one obtained with pure CO(2), and there was no significant difference in the biomass protein content. With D 0.8 d(-1), it was possible to obtain 56% +/- 1.5% and 50% +/- 1.2% of protein in the dry biomass, using pure CO(2) and CO(2) from alcoholic fermentation, respectively. These results demonstrate that the use of such cost free CO(2) from alcoholic fermentation as carbon source, associated with low cost nitrogen source, may be a promising way to reduce costs of continuous cultivation of photosynthetic microorganisms, contributing at the same time to mitigate the greenhouse effect. (C) 2011 American Institute of Chemical Engineers Biotechnol. Prog., 27: 650-656, 2011

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This work is focused on the influence of dilution rate (0.08 <= D <= 0.32 d(1)) on the continuous cultivation and biomass composition of Arthrospira (Spirulina) platensis using three different concentrations of ammonium chloride (c(No) = 1.0, 5.0 and 10 mol m (3)) as nitrogen source. At c(No) = 1.0 and 5.0 mol m (3) the biomass protein content was an increasing function of D, whereas, when using c(No) = 10 mol m (3), the highest protein content (72.5%) was obtained at D = 0.12 d (1). An overall evaluation of the process showed that biomass protein content increased with the rate of nitrogen supply (D c(No)) up to 72.5% at D c(No) = 1.20 mol m (3) d (1). Biomass lipid content was an increasing function of D only when the nitrogen source was the limiting factor for the growth (D c(No) <= 0.32 mol m (-3) d (1)), which occurred solely with c(No), = 1.0 mol m (3). Under such conditions, A. platensis reduced its nitrogen reserve in the form of proteins, while maintaining almost unvaried its lipid content. The latter was affected only when the concentration of nitrogen was extremely low (c(No) = 1.0 mol m (3)). The most abundant fatty acids were the palmitic (45.8 +/- 5.20%) and the gamma-linolenic (20.1 +/- 2.00%) ones. No significant alteration in the profiles either of saturated or unsaturated fatty acids was observed with c(No) <= 5.0 mol m (3), prevailing those with 16 and 18 carbons. (C) 2010 Elsevier Ltd. All rights reserved.

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Arthospira (Spirulina) platensis (Nordstedt) Gomont was autotrophically cultivated for biomass production in repeated fed-batch process using urea as nitrogen source, with the aim of making large-scale production easier, increasing cell productivity and then reducing the production costs. It was investigated the influence or the ratio of renewed volume to total volume (R), the Urea feeding time (t(f)) and the number of successive repealed fed-batch cycles on the maximum cell concentration (X(m)), cell productivity (P(x)), nitrogen-to-cell conversion yield (Y(x/n)), maximum specific growth rate (mu(m)) and protein content of, dry biomass. The experimental results demonstrated chat R=0.80 and t(f) = 6d were the best cultivation conditions, being able to simultaneously ensure, throughout the three fed-batch cycles, the highest average values of three of the five responses (X(m) = 2101 +/- 113 mg L(-1), P(x) = 219 +/- 13 mg L(-1) d(-1) and Y(x/n) = 10.3 +/- 0.8,g g(-1)). (C) 2008 Elsevier B.V. All rights reserved.

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The postharvest development of crown rot of bananas depends notably on the fruit susceptibility to this disease at harvest. It has been shown that fruit susceptibility to crown rot is variable and it was suggested that this depends on environmental preharvest factors. However, little is known about the preharvest factors influencing this susceptibility. The aim of this work was to evaluate the extent to which fruit filling characteristics during growth and the fruit development stage influence the banana susceptibility to crown rot. This involved evaluating the influence of (a) the fruit position at different levels of the banana bunch (hands) and (b) changing the source-sink ratio (So-Si ratio), on the fruit susceptibility to crown rot. The fruit susceptibility was determined by measuring the internal necrotic surface (INS) after artificial inoculation of Colletotrichum musae. A linear correlation (r = -0.95) was found between the hand position on the bunch and the INS. The So-Si ratio was found to influence the pomological characteristics of the fruits and their susceptibility to crown rot. Fruits of bunches from which six hands were removed (two hands remaining on the bunch) proved to be significantly less susceptible to crown rot (INS = 138.3 mm 2) than those from bunches with eight hands (INS = 237.9 mm 2). The banana susceptibility to crown rot is thus likely to be influenced by the fruit development stage and filling characteristics. The present results highlight the importance of standardising hand sampling on a bunch when testing fruit susceptibility to crown rot. They also show that hand removal in the field has advantages in the context of integrated pest management, making it possible to reduce fruit susceptibility to crown rot while increasing fruit size.

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Recently, we have built a classification model that is capable of assigning a given sesquiterpene lactone (STL) into exactly one tribe of the plant family Asteraceae from which the STL has been isolated. Although many plant species are able to biosynthesize a set of peculiar compounds, the occurrence of the same secondary metabolites in more than one tribe of Asteraceae is frequent. Building on our previous work, in this paper, we explore the possibility of assigning an STL to more than one tribe (class) simultaneously. When an object may belong to more than one class simultaneously, it is called multilabeled. In this work, we present a general overview of the techniques available to examine multilabeled data. The problem of evaluating the performance of a multilabeled classifier is discussed. Two particular multilabeled classification methods-cross-training with support vector machines (ct-SVM) and multilabeled k-nearest neighbors (M-L-kNN)were applied to the classification of the STLs into seven tribes from the plant family Asteraceae. The results are compared to a single-label classification and are analyzed from a chemotaxonomic point of view. The multilabeled approach allowed us to (1) model the reality as closely as possible, (2) improve our understanding of the relationship between the secondary metabolite profiles of different Asteraceae tribes, and (3) significantly decrease the number of plant sources to be considered for finding a certain STL. The presented classification models are useful for the targeted collection of plants with the objective of finding plant sources of natural compounds that are biologically active or possess other specific properties of interest.

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The University of Queensland, Australia has developed Fez, a world-leading user-interface and management system for Fedora-based institutional repositories, which bridges the gap between a repository and users. Christiaan Kortekaas, Andrew Bennett and Keith Webster will review this open source software that gives institutions the power to create a comprehensive repository solution without the hassle..

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Two basic representations of principal-agent relationships, the 'state-space' and 'parameterized distribution' formulations, have emerged. Although the state-space formulation appears more natural, analytical studies using this formulation have had limited success. This paper develops a state-space formulation of the moral-hazard problem using a general representation of production under uncertainty. A closed-form solution for the agency-cost problem is derived. Comparative-static results are deduced. Next we solve the principal's problem of selecting the optimal output given the agency-cost function. The analysis is applied to the problem of point-source pollution control. (C) 1998 Published by Elsevier Science S.A. All rights reserved.

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Crystals of recombinant importin alpha, the nuclear-import receptor, have been obtained at two different pH conditions by vapour diffusion using sodium citrate as precipitant and dithiothreitol as an additive. At pH 4-5, the crystals have the symmetry of the trigonal space group P3(1)21 or P3(2)21 (a = b = 78.0, c = 255.8 Angstrom, gamma = 120 degrees); at pH 6-7, the crystals have the symmetry of the orthorhombic space group P2(1)2(1)2(1) (a = 78.5, b = 89.7, c = 100.5 Angstrom). In both cases, there is probably one molecule of importin ct in the asymmetric unit. At least one of the crystal forms diffracts to a resolution higher than 3 Angstrom using the laboratory X-ray source; the crystals are suitable for crystal structure determination.

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Importin alpha is the nuclear import receptor that recognizes classical monopartite and bipartite nuclear localization signals (NLSs). The structure of mouse importin alpha has been determined at 2.5 Angstrom resolution. The structure shows a large C-terminal domain containing armadillo repeats, and a less structured N-terminal importin beta-binding domain containing an internal NLS bound to the NLS-binding site. The structure explains the regulatory switch between the cytoplasmic, high-affinity form, and the nuclear, low-affinity form for NLS binding of the nuclear import receptor predicted by the current models of nuclear import. Importin beta conceivably converts the low- to high-affinity form by binding to a site overlapping the autoinhibitory sequence. The structure also has implications for understanding NLS recognition, and the structures of armadillo and HEAT repeats.

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Human acetyl coenzyme A-dependent N-acetyltransferase (EC 2.3.1.5) (NAT) catalyzes the biotransformation of a number of arylamine and hydrazine compounds. NAT isozymes are encoded at 2 loci; one encodes NAT1, formerly known as the monomorphic form of the enzyme, while the other encodes the polymorphic NAT2, which is responsible for individual differences in the ability to acetylate certain compounds. Human epidemiological studies have suggested an association between the acetylator phenotype and particular cancers such as those of the bladder and colon. In the present study, NAT1- and NAT2-specific riboprobes were used in hybridization histochemistry studies to localize NAT1 and NAT2 mRNA sequences in formalin-fixed, paraffin-embedded human tissue sections. Expression of both NAT1 and NAT2 mRNA was observed in liver, gastrointestinal tract tissues (esophagus, stomach, small intestine, and colon), ureter, bladder, and lung. In extrahepatic tissues, NAT1 and NAT2 mRNA expression was localized to intestinal epithelial cells, urothelial cells, and the epithelial cells of the respiratory bronchioles. The observed heterogeneity of NAT1 and NAT2 mRNA expression between human tissue types may be of significance in assessing their contribution to known organ-specific toxicities of various arylamine drugs and carcinogens.

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Induction of apoptosis in cells by TNF-related apoptosis-inducing ligand (TRAIL), a member of the TNF family, is believed to be regulated by expression of two death-inducing and two inhibitory (decoy) receptors on the cell surface. In previous studies we found no correlation between expression of decoy receptors and susceptibility of human melanoma cells to TRAIL-induced apoptosis, In view of this, we studied the localization of the receptors in melanoma cells by confocal microscopy to better understand their function. We show that the death receptors TRAIL-R1 and R2 are located in the trans-Golgi network, whereas the inhibitory receptors TRAIL-R3 and -R4 are located in the nucleus. After exposure to TRAIL, TRAIL-R1 and -R2 are internalized into endosomes, whereas TRAIL-R3 and -R4 undergo relocation from the nucleus to the cytoplasm and cell membranes. This movement of decoy receptors was dependent on signals from TRAIL-R1 and -R2, as shown by blocking experiments with Abs to TRAIL-R1 and -R2, The location of TRAIL-R1, -R3, and -R4 in melanoma cells transfected with cDNA for these receptors was similar to that in nontransfected cells, Transfection of TRAIL-R3 and -R4 increased resistance of the melanoma lines to TRAIL-induced apoptosis even in melanoma lines that naturally expressed these receptors. These results indicate that abnormalities in decoy receptor location or function may contribute to sensitivity of melanoma to TRAIL-induced apoptosis and suggest that further studies are needed on the functional significance of their nuclear location and TRAIL-induced movement within cell.

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Importin-alpha is the nuclear import receptor that recognizes cargo proteins which contain classical monopartite and bipartite nuclear localization sequences (NLSs), and facilitates their transport into the nucleus. To determine the structural basis of the recognition of the two classes of NLSs by mammalian importin-alpha, we co-crystallized an N-terminally truncated mouse receptor protein with peptides corresponding to the monopartite NLS from the simian virus 40 (SV40) large T-antigen, and the bipartite NLS from nucleoplasmin. We show that the monopartite SV40 large T-antigen NLS binds to two binding sites on the receptor, similar to what was observed in yeast importin-alpha. The nucleoplasmin NLS-importin-alpha complex shows, for the first time, the mode of binding of bipartite NLSs to the receptor. The two basic clusters in the NLS occupy the two binding sites used by the monopartite NLS, while the sequence linking the two basic clusters is poorly ordered, consistent with its tolerance to mutations. The structures explain the structural basis for binding of diverse NLSs to the sole receptor protein. (C) 2000 Academic Press.