Registro completo de metadatos
Campo DC Valor Lengua/Idioma
dc.creatorCarjuzaa, P.-
dc.creatorCastellion, Martina Laura-
dc.creatorDistéfano, Ana Julia-
dc.creatordel Vas, Mariana-
dc.creatorMaldonado, Sara Beatriz-
dc.date2019-01-08T16:07:49Z-
dc.date2019-01-08T16:07:49Z-
dc.date2008-09-
dc.date2019-01-02T18:28:43Z-
dc.date.accessioned2019-04-29T15:55:50Z-
dc.date.available2019-04-29T15:55:50Z-
dc.identifierCarjuzaa, P.; Castellion, Martina Laura; Distéfano, Ana Julia; del Vas, Mariana; Maldonado, Sara Beatriz; Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos; Springer Wien; Protoplasma; 233; 1-2; 9-2008; 149-156-
dc.identifier0033-183X-
dc.identifierhttp://hdl.handle.net/11336/67660-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/305594-
dc.descriptionThe aim of this study was to characterize the dehydrin content in mature embryos of two quinoa cultivars, Sajama and Baer La Unión. Cultivar Sajama grows at 3600-4000 m altitude and is adapted to the very arid conditions characteristic of the salty soils of the Bolivian Altiplano, with less than 250 mm of annual rain and a minimum temperature of -1 °C. Cultivar Baer La Unión grows at sea-level regions of central Chile and is adapted to more humid conditions (800 to 1500 mm of annual rain), fertile soils, and temperatures above 5 °C. Western blot analysis of embryo tissues from plants growing under controlled greenhouse conditions clearly revealed the presence of several dehydrin bands (at molecular masses of approximately 30, 32, 50, and 55 kDa), which were common to both cultivars, although the amount of the 30 and 32 kDa bands differed. Nevertheless, when grains originated from their respective natural environments, three extra bands (at molecular masses of approximately 34, 38, and 40 kDa), which were hardly visible in Sajama, and another weak band (at a molecular mass of approximately 28 kDa) were evident in Baer La Unión. In situ immunolocalization microscopy detected dehydrin-like proteins in all axis and cotyledon tissues. At the subcellular level, dehydrins were detected in the plasma membrane, cytoplasm and nucleus. In the cytoplasm, dehydrins were found associated with mitochondria, rough endoplasmic reticulum cisternae, and proplastid membranes. The presence of dehydrins was also recognized in the matrix of protein bodies. In the nucleus, dehydrins were associated with the euchromatin. Upon examining dehydrin composition and subcellular localization in two quinoa cultivars belonging to highly contrasting environments, we conclude that most dehydrins detected here were constitutive components of the quinoa seed developmental program, but some of them (specially the 34, 38, and 40 kDa bands) may reflect quantitative molecular differences associated with the adaptation of both cultivars to contrasting environmental conditions. © 2008 Springer-Verlag.-
dc.descriptionFil: Carjuzaa, P.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina-
dc.descriptionFil: Castellion, Martina Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina-
dc.descriptionFil: Distéfano, Ana Julia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina-
dc.descriptionFil: del Vas, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina-
dc.descriptionFil: Maldonado, Sara Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Recursos Biológicos; Argentina-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherSpringer Wien-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1007/s00709-008-0300-4-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00709-008-0300-4-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectCHENOPODIUM QUINOA-
dc.subjectDEHYDRIN-
dc.subjectENVIRONMENT-
dc.subjectIN SITU IMMUNOLOCALIZATION-
dc.subjectQUINOA CULTIVAR-
dc.subjectWESTERN BLOT ANALYSIS-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleDetection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: CONICET

Ficheros en este ítem:
No hay ficheros asociados a este ítem.