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                <text>&lt;strong&gt;Electrophoretic mobility : primary electroviscous effect and colloid stability of highly charged polystyrene latexes&lt;/strong&gt;</text>
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                <text>LATEX DE POLIESTIRENO</text>
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                <text>Negatively charged polystyrene latexes with relatively high surface charge density have been prepared by the emulsifier-free method. Three samples of approximately the same particle size and different surface charge density have been obtained. The effect of pH and ionic strength on electrophoretic mobility has been studied and the experimental mobility converted into &amp;zeta;-potential according to the O&amp;rsquo;Brien-White and Dukhin-Semenikhin theoretical treatments. &amp;mdash; The &amp;zeta;-potential values obtained by D-S equation are reasonably in agreement with the predictions of the Gouy-Chapman model. Thus, the passage of mobility and, correspondingly, &amp;zeta;-potential through a maximum at low ionic strengths of the solution is due to the influence of surface conductance on electrophoresis. Also, primary electroviscous effect has been measured. An approximate equation derived from Booth theory explained the variation of the relative viscosity with the electrokinetic radius. The agreement between theory and experimental data was very good. Finally, critical coagulation concentration values were obtained experimentally. No significant differences were found, whcih is in agreement with the similar &amp;zeta;-potential values obtained with the three samples of polystyrene latex.</text>
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                <text>&lt;strong&gt;Chabalgoity, Alejandro&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Mart&amp;iacute;n, A.&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Galisteo, F.&lt;/strong&gt;</text>
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                <text>Progress in Colloid and Polymer Science |g v. 84, , 1991. -- p. 416-424</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>DOI: 10.1007/BFb0116015</text>
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                <text>&lt;strong&gt;A Salmonella typhimurium htrA live vaccine expressing multiple copies of a peptide comprising amino acids 8-23 of herpes simplex virus glycoprotein D as a genetic fusion to tetanus toxin fragment C protect mice from herpes simplex virus infection.&lt;br /&gt;&lt;/strong&gt;</text>
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                <text>Multiple tandem copies of an immunogenic epitope comprising amino acids 8&amp;ndash;23 of glycoprotein D of herpes simplex virus (HSV) were expressed as C-terminal fusions to tetanus toxin fragment C (TetC) in different Salmonella typhimurium live vaccine strains. Expression of the longer fusions was best in strains harbouring a lesion in htrA, a stress protein gene. SL3261, an aroA strain, did not effectively express the longer fusions. Mice immunised with an S. typhimurium C5 htrA mutant expressing fusions with two or four copies of the peptide made an antibody response to both the peptide and TetC, whereas constructs expressing one copy of the peptide only elicited antibody to TetC. A non-immunogenic octameric fusion underwent rearrangements in vivo resulting in a predominantly monomeric fusion. In contrast, the S. typhimurium SL3261 aroA vaccine expressing the TetC-tetrameric fusion did not elicit antibody to the peptide. Sera from mice immunised with a single dose of the dimer and tetramer fusions in the htrA strain neutralised HSV in vitro, and the mice were protected from HSV infection as measured by a reduction in virus load in the ear pinna. We have previously shown that mice vaccinated with salmonella expressing TetC are protected against tetanus toxin and virulent salmonella challenge. These results suggest that it may be possible to develop a multivalent vaccine against salmonellosis, tetanus and HSV.</text>
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                <text>&lt;strong&gt;Chabalgoity, J A&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Hormaeche, C&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Khan, C&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Nash, A&lt;/strong&gt;</text>
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                <text>Molecular Microbiology v. 19, no. 4, 1996. -- p. 791-886</text>
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              <elementText elementTextId="328323">
                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya&lt;/strong&gt; protege el derecho de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes&lt;/p&gt;&#13;
&lt;p&gt;(LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;&#13;
&lt;p&gt;&amp;nbsp;&lt;/p&gt;</text>
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                <text>A live attenuated Salmonella typhimurium vaccine candidate, LVR01, was constructed by introducing a null deletion into the aroC gene of the parental canine S. typhimurium isolate, P228067. LVR01 was used to orally deliver to the canine immune system a fatty acid binding protein (FABP) from Echinococcus granulosus (EgDf1), as a fusion protein with fragment C (TetC) of tetanus toxin. Immunization studies demonstrated that live LVR01 is well tolerated by orally vaccinated dogs. There was no detectable shedding of the vaccine strain in the faeces 2 days after immunization. Humoral antibody responses were observed against Salmonella, TetC and EgDf1. Cellular responses were consistently detected against Salmonella and TetC. A cellular response against EgDf1 was also seen in a proportion of the LVR01 vaccinated dogs. We propose S. typhimurium LVR01 as a carrier for recombinant antigens and a vector for the construction of multivalent oral vaccines for dogs.</text>
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                <text>&lt;strong&gt;Moreno, M.&lt;/strong&gt;</text>
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                <text>Vaccine v. 19, , 2000. -- p. 460-469</text>
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                <text>Cytokines are key regulators of the immune system that shape innate and adaptive immune responses. An adequate balance of the cytokine environment is critical to achieve protective immunity and to avoid immunopathology. Present knowledge allows a deeper understanding of the cytokine network and their sometimes conflicting roles in the development of immune responses, as well as their relevance in the establishment and maintenance of immunological memory. New insights have been gained into the role of different T cell subsets for protection against infection or tumor growth. The incorporation of cytokines as molecular adjuvants in vaccines has been attempted to strengthen vaccine-induced immune responses, and as a rational approach to modulate cytokine milieu in vivo and tailor host immunity for specific situations. These approaches have been tried in experimental models and veterinary species, and a few of them have entered into clinical trials. However, manipulating the cytokine network to modulate immune responses is not a simple task, because cytokine functions are complex and the final effects on the immune response will depend on timing and length of exposure, cell(s) targeted and other cytokines present in the same microenvironment. Here, we will review our present understanding on the role of cytokines in the development of effector and memory T cell responses. Also the potential use of cytokines as molecular adjuvant for vaccines against infectious diseases and cancer will be revised.</text>
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                <text>&lt;strong&gt;Chabalgoity, Jose A.&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Baz, Adriana&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Rial, Anal&amp;iacute;a&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Grille, Sof&amp;iacute;a&lt;/strong&gt;</text>
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                <text>Cytokine and Growth Factor Reviews v. 18, no. 1-2, 2007. -- p.195-207</text>
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                <text>Elsevier</text>
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                <text>2007</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>DOI:10.1016/j.cytogfr.2007.01.016</text>
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                <text>Fatty acid-binding proteins (FABPs) are candidate molecules for vaccines against several parasitic platyhelminths. A FABP from the cestode Echinococcus granulosus (EgDf1) was expressed in Salmonella vaccine strains as a C-terminal fusion to fragment C of tetanus toxin (TetC) by using expression vector pTECH. The fusion protein was equally expressed in several attenuated vaccine strains derived from bacteria with different genetic backgrounds and different attenuating mutations. Single-dose immunization experiments with the aroA Salmonella typhimurium strain SL3261 carrying the pTECH-EgDf1 construct were conducted with mice, using both the intravenous and the oral routes. Surprisingly, the antibody response to EgDf1 and the antigen-specific cytokine production in spleen cells were stronger in mice immunized orally. Furthermore, immune mouse sera strongly reacted with fixed sections of the worm's larval stage. Analysis of the isotype distribution of the specific anti-EgDf1 antibodies showed similar production of immunoglobulin G1 (IgG1) and IgG2a together with specific IgA antibodies. In addition, stimulation of spleen cells from mice immunized with the different constructs with either Salmonella lysate, TetC, or EgDf1 showed that, together with Th1-related cytokines (gamma interferon and interleukin 2 [IL-2]), significant levels of a Th2 cytokine (IL-5) were produced specifically, indicating a Th2 component to the response to the Salmonella carrier and to the recombinant antigens. Salmonellae expressing the TetC-rEgDfl fusion are currently under evaluation as potential vaccines against E. granulosus.</text>
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                <text>he insert of a clone from a &amp;lambda;gt11 Echinococcus granulosus (Platyhelminth, Cestoda) protoscolex cDNA library, showed an open reading frame whose deduced protein sequence presents a high homology with all described thioredoxins (TRX). The TRX active site (Trp-Cys-Gly-Pro-Cys) is completely conserved. With a monospecific antibody, selected from a total anti-protoscolex sera by the isolated clone, a 12 kDa polypeptide was immunoprecipitated from a protoscolex total protein extract. Furthermore, an antiserum raised against a recombinant EgTRX also recognizes a 12 kDa band in these extracts. The recombinant protein presents TRX activity, using the insulin reduction assay. Finally, a TRX activity was characterized in protoscolex extracts. In all organisms where TRXs were studied, they participate in a cascade of redox exchanges, contributing to the maintaining of cell homeostasis. Considering that the parasitic flatworm E. granulosus is probably submitted to an important oxidative stress due to host defences, EgTRX protein could be involved in the survival strategies of this parasite.</text>
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>Minireviews Reports Classics Reflections Papers of the Week QUICK SEARCHAuthor:Keyword:Year:Vol:Page:GO [Advanced Search][Browse the Archive] Advertisement Advertisement JBC's Young Investigator Award: Learn More Alternative mRNAs Arising from Trans-splicing Code for Mitochondrial and Cytosolic Variants of Echinococcus granulosus Thioredoxin Glutathione Reductase* Astrid Agorio&amp;Dagger;&amp;sect;, Cora Chalar&amp;para;, Soledad Cardozo&amp;Dagger; and Gustavo Salinas&amp;Dagger;‖ + Author Affiliations From the &amp;Dagger;C&amp;aacute;tedra de Inmunologı́a, Facultad de Quı́mica/Ciencias, Universidad de la Rep&amp;uacute;blica, Avenida Alfredo Navarro 3051, Piso 2, CP 11.600, Montevideo, Uruguay and &amp;para;Secci&amp;oacute;n Bioquı́mica, Facultad de Ciencias, Universidad de la Rep&amp;uacute;blica, Igu&amp;aacute;4225, CP 11.500, Montevideo, Uruguay Next Section Abstract Thioredoxin and glutathione systems are the major thiol-dependent redox systems in animal cells. They transfer via the reversible oxidoreduction of thiols the reducing equivalents of NADPH to numerous substrates and substrate reductases and constitute major defenses against oxidative stress. In this study, we cloned from the helminth parasite Echinococcus granulosus two trans-spliced mRNA variants that encode thioredoxin glutathione reductases (TGR). These variants code for mitochondrial and cytosolic selenocysteine-containing isoforms that possess identical glutaredoxin (Grx) and thioredoxin reductase (TR) domains and differ exclusively in their N termini. Western blot analysis of subcellular fractions with specific anti-TGR antibodies showed that TGR is present in both compartments. The biochemical characterization of the native purified TGR suggests that the Grx and TR domains of the enzyme can function either coupled or independently of each other, because the Grx domain can accept electrons from either TR domains or the glutathione system and the TR domains can transfer electrons to either the fused Grx domain or to E. granulosus thioredoxin. The reversible thiol-disulfide reaction is a central theme in biology. On the one hand, this redox exchange is an efficient mechanism of electron transport. On the other hand, this reaction is a molecular device used by nature as a switch to control protein function and localization through the redox state of critical thiol groups (1). The central role in thiol-disulfide exchange in animal cells is played by the thioredoxin (Trx)1 and glutathione (GSH) systems. Both systems have overlapping and distinct properties and targets but function in a similar way. They transfer via the reversible oxidoreduction of thiols the reducing equivalents of NADPH to numerous substrates and substrate reductases (2). They maintain the cellular redox homeostasis and constitute major defenses against oxidative stress, acting directly by reducing oxidized compounds and proteins or providing reducing equivalents to the hydrogen peroxide reductases present in animal cells, namely thioredoxin peroxidase and glutathione peroxidase (3). Both systems provide electrons to ribonucleotide reductase and control vital cellular processes such as transcription and signal transduction through the redox regulation of kinases, phosphatases, and transcription factors (4-6). The animal thioredoxin system comprises the thioredoxin reductase (TR) and Trx, whereas the glutathione system consists of glutathione reductase (GR), glutathione (GSH), and glutaredoxin (Grx). Trx and Grx are thiol-disulfide oxidoreductases that transfer electrons to various substrates and substrates reductases. GSH, another thiol-based reductant, recycles Grx to its reduced state and reduces other protein and non-protein substrates. TR and GR are pyridine nucleotide-disulfide oxidoreductases that transfer the reducing equivalents of NADPH to oxidized Trx and other substrates and to GSH, respectively. Mammalian and Caenorhabditis elegans TR possess C-terminal electron transfer centers containing redox active cysteine and selenocysteine (Sec) residues (7-10). The selenol group of Sec is a strong nucleophile (11) that confers a profound reductive capacity to the enzyme. The C-terminal redox center is not present in GR. The equivalent redox link in the GSH system is thought to be provided by GSH (10). In mammals, both systems are present in mitochondria and the cytosol. This is because of the existence of genes encoding mitochondrial and cytosolic variants for the proteins from both systems and also because of alternative splicing of single genes (12-17). Recently, mitochondrial and cytosolic variants of DrosophilaTR have also been described to be derived from alternative splicing of a single gene (18). Recently, a more complex machine exhibiting specificity for both thioredoxin and glutathione systems has been characterized in mammals (19). This enzyme termed thioredoxin glutathione reductase (TGR) is a selenoprotein oxidoreductase that possesses thioredoxin reductase, glutathione reductase, and glutaredoxin activities, achieving this broad substrate specificity by a fusion of TR and Grx domains. This enzyme has been reported to be present in the microsomal fraction of testis cells from mice. A multifunctional TGR has also been reported inSchistosoma mansoni, a platyhelminth organism (20), indicating that this fusion domain has been evolutionarily conserved. In this article, we report the cloning and characterization of a thioredoxin glutathione reductase of the larval stage ofEchinococcus granulosus, a cestode parasite that dwells in the liver and lungs of human and cattle hosts. The results indicate that the enzyme possesses glutathione reductase, thioredoxin reductase, and glutaredoxin activities and suggest that there is domain communication between the C-terminal Cys-Sec redox center and the N-terminal glutaredoxin domain. In addition, we provide conclusive evidence that mitochondrial and cytosolic variants of TGR are generated from a single TGR gene</text>
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt; La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt; de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>Five groups of Wistar rats were subcutaneously infected with 5000 L3 stage larvae of Nippostronzgylils brasilietisis. Four groups were dosed orally with 5, 10, 15, and 20 mg/kg body weight of albendazole at 5 h postinfection, and one group served as an untreated control. The animals were euthanized and the intestines were dissected out 72 h postinfection and were incubated on a Baermann's apparatus to recover L4 stage larvae. No larvae were recovered from the 20 mg/kg albendazole-treated group, and means of 15, 33, and 175 L4 larvae were recovered from the 15, 10, and 5 mg/kg albendazole-treated groups, respectively. Levamisole and fenbendazole were also tested using the same procedure. Means of 100 and 1887 L4 larvae were obtained from the 50 and 10 mg/kg of levamisole-treated groups respectively; while, 191 and 583 L4 larvae were recovered from rats treated with 50 and 10 mg/kg of fenbendazole, respectively. These results indicate that the L4 stage of N. brasiliensis could be useful for in vivo screening of new nematocide drugs.</text>
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                <text>&lt;strong&gt;Dominguez, L&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Saldana, J&lt;/strong&gt;</text>
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                <text>Canadian Journal of Veterinary Research = Revue canadiennede recherche v&amp;eacute;t&amp;eacute;rinaire&amp;nbsp; v. 64, no. 3, 2000. -- p. 160-163</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt;&amp;nbsp;La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>Ph : &amp;Oacute;rgano Oficial de la Asociaci&amp;oacute;n de Estudiantes de Qu&amp;iacute;mica Uruguay n&amp;ordm;. 2, 1940. -- p. 34-35</text>
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                <text>Asociaci&amp;oacute;n de Estudiantes de Qu&amp;iacute;mica (Uruguay)</text>
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                <text>1940</text>
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                <text>&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;br /&gt;&lt;br /&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;br /&gt;&lt;br /&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya&lt;/strong&gt; protege el derecho de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes&lt;br /&gt;&lt;br /&gt;(LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)&lt;br /&gt;&lt;br /&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.</text>
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