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dc.contributor.author
Rosa, Mariana Daniela

dc.contributor.author
Hilal, Mirna Beatriz

dc.contributor.author
González, Juan Antonio

dc.contributor.author
Prado, Fernando Eduardo

dc.date.available
2019-05-06T22:02:45Z
dc.date.issued
2009-04
dc.identifier.citation
Rosa, Mariana Daniela; Hilal, Mirna Beatriz; González, Juan Antonio; Prado, Fernando Eduardo; Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings; Elsevier Masson; Plant Physiology and Biochemistry; 47; 4; 4-2009; 300-307
dc.identifier.issn
0981-9428
dc.identifier.uri
http://hdl.handle.net/11336/75714
dc.description.abstract
The effect of low temperature on growth, sucrose-starch partitioning and related enzymes in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) was studied. The growth of cotyledons and growing axes in seedlings grown at 25/20 °C (light/dark) and shifted to 5/5 °C was lower than in those only growing at 25/20 °C (unstressed). However, there were no significant differences between low-temperature control and salt-treated seedlings. The higher activities of sucrose phosphate synthase (SPS, EC 2.4.1.14) and soluble acid invertase (acid INV, EC 3.2.1.25) were observed in salt-stressed cotyledons; however, the highest acid INV activity was observed in unstressed cotyledons. ADP-glucose pyrophosphorylase (ADP-GPPase, EC 2.7.7.27) was higher in unstressed cotyledons than in stressed ones. However, between 0 and 4 days the highest value was observed in salt-stressed cotyledons. The lowest value of ADP-GPPase was observed in salt-acclimated cotyledons. Low temperature also affected sucrose synthase (SuSy, EC 2.4.1.13) activity in salt-treated cotyledons. Sucrose and glucose were higher in salt-stressed cotyledons, but fructose was essentially higher in low-temperature control. Starch was higher in low-temperature control; however, the highest content was observed at 0 day in salt-acclimated cotyledons. Results demonstrated that low temperature induces different responses on sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons. Data also suggest that in salt-treated cotyledons source-sink relations (SSR) are changed in order to supply soluble sugars and proline for the osmotic adjustment. Relationships between starch formation and SuSy activity are also discussed.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Masson

dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Acid Invertase
dc.subject
Adp-Glucose Pyrophosphorylase
dc.subject
Chenopodium Quinoa
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Sucrose Phosphate Synthase
dc.subject
Sucrose Synthase
dc.subject
Sucrose-Starch Partitioning
dc.subject.classification
Otras Ciencias Biológicas

dc.subject.classification
Ciencias Biológicas

dc.subject.classification
CIENCIAS NATURALES Y EXACTAS

dc.title
Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-04-23T17:52:42Z
dc.journal.volume
47
dc.journal.number
4
dc.journal.pagination
300-307
dc.journal.pais
Francia

dc.description.fil
Fil: Rosa, Mariana Daniela. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Hilal, Mirna Beatriz. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: González, Juan Antonio. Fundación Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Prado, Fernando Eduardo. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title
Plant Physiology and Biochemistry

dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.plaphy.2008.12.001
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0981942808002350
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