Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings
- Autores
- Rosa, Mariana Daniela; Hilal, Mirna Beatriz; González, Juan Antonio; Prado, Fernando Eduardo
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
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
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
Fil: González, Juan Antonio. Fundación Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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 - Materia
-
Acid Invertase
Adp-Glucose Pyrophosphorylase
Chenopodium Quinoa
Sucrose Phosphate Synthase
Sucrose Synthase
Sucrose-Starch Partitioning - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/75714
Ver los metadatos del registro completo
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CONICET Digital (CONICET) |
spelling |
Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlingsRosa, Mariana DanielaHilal, Mirna BeatrizGonzález, Juan AntonioPrado, Fernando EduardoAcid InvertaseAdp-Glucose PyrophosphorylaseChenopodium QuinoaSucrose Phosphate SynthaseSucrose SynthaseSucrose-Starch Partitioninghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The 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.Fil: Rosa, Mariana Daniela. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Hilal, Mirna Beatriz. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: González, Juan Antonio. Fundación Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Prado, Fernando Eduardo. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Masson2009-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/75714Rosa, 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; 300-3070981-9428CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.plaphy.2008.12.001info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0981942808002350info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:03:42Zoai:ri.conicet.gov.ar:11336/75714instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:03:42.64CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings |
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 |
spellingShingle |
Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings Rosa, Mariana Daniela Acid Invertase Adp-Glucose Pyrophosphorylase Chenopodium Quinoa Sucrose Phosphate Synthase Sucrose Synthase Sucrose-Starch Partitioning |
title_short |
Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings |
title_full |
Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings |
title_fullStr |
Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings |
title_full_unstemmed |
Low-temperature effect on enzyme activities involved in sucrose-starch partitioning in salt-stressed and salt-acclimated cotyledons of quinoa (Chenopodium quinoa Willd.) seedlings |
title_sort |
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.creator.none.fl_str_mv |
Rosa, Mariana Daniela Hilal, Mirna Beatriz González, Juan Antonio Prado, Fernando Eduardo |
author |
Rosa, Mariana Daniela |
author_facet |
Rosa, Mariana Daniela Hilal, Mirna Beatriz González, Juan Antonio Prado, Fernando Eduardo |
author_role |
author |
author2 |
Hilal, Mirna Beatriz González, Juan Antonio Prado, Fernando Eduardo |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Acid Invertase Adp-Glucose Pyrophosphorylase Chenopodium Quinoa Sucrose Phosphate Synthase Sucrose Synthase Sucrose-Starch Partitioning |
topic |
Acid Invertase Adp-Glucose Pyrophosphorylase Chenopodium Quinoa Sucrose Phosphate Synthase Sucrose Synthase Sucrose-Starch Partitioning |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
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. 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 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 Fil: González, Juan Antonio. Fundación Miguel Lillo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina 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 |
description |
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. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-04 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/75714 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 0981-9428 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/75714 |
identifier_str_mv |
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 0981-9428 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.plaphy.2008.12.001 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0981942808002350 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Masson |
publisher.none.fl_str_mv |
Elsevier Masson |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
_version_ |
1844613856707477504 |
score |
13.070432 |