Mostrar el registro sencillo del ítem

dc.contributor.author
Balestrasse, Karina Beatriz  
dc.contributor.author
Gallego, Susana Mabel  
dc.contributor.author
Tomaro, Maria Lujan  
dc.date.available
2021-04-23T13:58:04Z  
dc.date.issued
2006-12  
dc.identifier.citation
Balestrasse, Karina Beatriz; Gallego, Susana Mabel; Tomaro, Maria Lujan; Oxidation of the enzymes involved in nitrogen assimilation plays an important role in the cadmium-induced toxicity in soybean plants; Springer; Plant and Soil; 284; 1-2; 12-2006; 187-194  
dc.identifier.issn
0032-079X  
dc.identifier.uri
http://hdl.handle.net/11336/130767  
dc.description.abstract
Cadmium causes oxidative damage and hence affects nitrogen assimilation. In the present work we tested the relationship between the inactivation of the enzymes involved in nitrogen assimilation pathway (glutamine synthetase (GS)/glutamate synthase (GOGAT)) and the protein oxidation in nodules of soybean (Glycine max L.) plants under Cd2+ stress. Therefore, the effect of Cd2+ and reduced gluthatione (GSH) on GS and GOGAT activities, and protein abundance and oxidation were analyzed. Under the metal treatment, amino acids oxidative modification occurred, evidenced by the accumulation of carbonylated proteins, especially those of high molecular weight. When Cd 2+ was present in the nutrient solution, although a decrease in GS and GOGAT activities was observed (17 and 52%, respectively, compared to controls), the protein abundance of both enzymes remained similar to control nodules. When GSH was added together with Cd2+ in the nutrient medium, it protected the nodule against Cd2+ induced oxidative damage, maintaining GS and GOGAT activities close to control values. These results allow us to conclude that the inactivation of the nitrogen assimilation pathway by Cd2+ in soybean nodules is due to an increment in GS and GOGAT oxidation that can be prevented by the soluble antioxidant GSH.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Springer  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
BRADYRHIZOBIUM JAPONICUM  
dc.subject
CADMIUM  
dc.subject
GLYCINE MAX L.  
dc.subject
NITROGEN ASSIMILATION  
dc.subject
PROTEIN OXIDATION  
dc.subject.classification
Otras Ciencias Químicas  
dc.subject.classification
Ciencias Químicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
Oxidation of the enzymes involved in nitrogen assimilation plays an important role in the cadmium-induced toxicity in soybean plants  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2020-07-21T20:21:51Z  
dc.journal.volume
284  
dc.journal.number
1-2  
dc.journal.pagination
187-194  
dc.journal.pais
Alemania  
dc.journal.ciudad
Berlín  
dc.description.fil
Fil: Balestrasse, Karina Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Grupo Vinculado Centro de Estudios de Biodiversidad y Biotecnología MdP- INBA; Argentina  
dc.description.fil
Fil: Gallego, Susana Mabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina  
dc.description.fil
Fil: Tomaro, Maria Lujan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Centro de Investigaciones sobre Porfirinas y Porfirias. Universidad de Buenos Aires. Centro de Investigaciones sobre Porfirinas y Porfirias; Argentina  
dc.journal.title
Plant and Soil  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s11104-006-0050-z  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s11104-006-0050-z