1 25 1 https://riquim.fq.edu.uy/files/original/25df25748a163195c01b98f648806f48.pdf 2c794d59f0973d399f1c882fe8173002 https://riquim.fq.edu.uy/files/original/e268a98ed577df316120bf1937985255.jpg 269c9157d12cc293b33d761eb2225b60 Omeka Image File The metadata element set that was included in the `files_images` table in previous versions of Omeka. These elements are common to all image files. Bit Depth 8 Channels 3 Height 200 Width 200 Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Bibliografía Nacional Química Description An account of the resource Contiene la producción científica nacional de los profesionales químicos e investigadores, durante el período 1929 hasta la fecha. Contributor An entity responsible for making contributions to the resource Departamento de Documentación y Biblioteca RIQUIM Document A resource containing textual data. Note that facsimiles or images of texts are still of the genre text. Original Format If the image is of an object, state the type of object, such as painting, sculpture, paper, photo, and additional data PDF Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Characterisation of the Native Lipid Moiety of Echinococcus granulosus Antigen B Subject The topic of the resource ECHINOCOCCUS GRANULOSUS BIOQUÍMICA LÍPIDOS ANTÍGENOS ENFERMEDADES PARASITARIAS BIBLIOGRAFÍA NACIONAL QUÍMICA 2012 Abstract A summary of the resource. Antigen B (EgAgB) is the most abundant and immunogenic antigen produced by the larval stage (metacestode) of Echinococcus granulosus. It is a lipoprotein, the structure and function of which have not been completely elucidated. EgAgB apolipoprotein components have been well characterised; they share homology with a group of hydrophobic ligand binding proteins (HLBPs) present exclusively in cestode organisms, and consist of different isoforms of 8-kDa proteins encoded by a polymorphic multigene family comprising five subfamilies (EgAgB1 to EgAgB5). In vitro studies have shown that EgAgB apolipoproteins are capable of binding fatty acids. However, the identity of the native lipid components of EgAgB remains unknown. The present work was aimed at characterising the lipid ligands bound to EgAgB in vivo. EgAgB was purified to homogeneity from hydatid cyst fluid and its lipid fraction was extracted using chloroform:methanol mixtures. This fraction constituted approximately 40–50% of EgAgB total mass. High-performance thin layer chromatography revealed that the native lipid moiety of EgAgB consists of a variety of neutral (mainly triacylglycerides, sterols and sterol esters) and polar (mainly phosphatidylcholine) lipids. Gas-liquid chromatography analysis showed that 16:0, 18:0 and 18:1(n-9) are the most abundant fatty acids in EgAgB. Furthermore, size exclusion chromatography coupled to light scattering demonstrated that EgAgB comprises a population of particles heterogeneous in size, with an average molecular mass of 229 kDa. Our results provide the first direct evidence of the nature of the hydrophobic ligands bound to EgAgB in vivo and indicate that the structure and composition of EgAgB lipoprotein particles are more complex than previously thought, resembling high density plasma lipoproteins. Results are discussed considering what is known on lipid metabolism in cestodes, and taken into account the Echinococcus spp. genomic information regarding both lipid metabolism and the EgAgB gene family. Creator An entity primarily responsible for making the resource Obal, Gonzalo Ramos, Ana Lía Silva, Valeria Lima, Analía Batthyany, Carlos Bessio, María Inés <a title="currículum vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=06ea8350d5f6e14cde5d4fa22f5ff626" target="_blank">Ferreira Chiesa, Fernando</a> <a href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=8b2cacb0aafc512133624fa7b9bf174c">Salinas, Gustavo</a> Ferreira, Ana María Source A related resource from which the described resource is derived PloS Neglected Tropical Diseases v. 6, no. 5, 2012. -- e.1642 Publisher An entity responsible for making the resource available Dalton, John Pius McGill University, Canada Date A point or period of time associated with an event in the lifecycle of the resource 2012 Rights Information about rights held in and over the resource La legislación uruguaya protege el derecho de autor sobre toda creación literaria, científica o artística, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeción a lo establecido por el derecho común 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) ADVERTENCIA - La consulta de este documento queda condicionada a la aceptación de las siguientes condiciones de uso: Este documento es únicamente para usos privados enmarcados en actividades de investigación y docencia. No se autoriza su reproducción con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilización o cita de partes debe indicarse el nombre de la persona autora. Format The file format, physical medium, or dimensions of the resource PDF Language A language of the resource Inglés Type The nature or genre of the resource Artículo Identifier An unambiguous reference to the resource within a given context ISSN 1935-2727 Antígenos Bioquímica Lipidos literatura científica uruguaya