An invertase inhibitory protein from Pteris deflexa link fronds

Autores
Sayago, Jorge Esteban; Vattuone, Marta Amelia; Sampietro, A. R.; Isla, Maria Ines
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Plant invertases play important roles in sucrose metabolism. Cell wall invertase was reported to participate in phloem loading and unloading. Soluble invertases would be involved in hexose level regulation in mature tissues and in stored sucrose utilization within vacuoles. Invertase inhibitory proteins were described as one of the possible mechanisms for invertase activity regulation in some plant species; nevertheless, these proteins were found only in sink tissues, suggesting that this mechanism would not be relevant in the sucrose turnover of leaves. This report describes the purification of invertase from Pteris deflexa fronds and the occurrence of an invertase inhibitory protein in this fern organ, as well as its purification and invertase-inhibitor interactions. The Mr of the invertase and of its inhibitory protein were 90,000 and 18,000, respectively. SDS-PAGE in the presence of 2-mercaptoetanol gave two subunits for the enzyme (Mr=66,000 and 30,000) and only one for the inhibitor. The inhibitor protein is a glycoprotein (12% w/w of neutral sugars) that did not show agglutinating activity like some others, and also showed a high heat stability at pH 5.0. The optimum pH of invertase activity is 5.0, while invertase inhibitory protein caused maximal inhibition at the same pH value. Invertase-inhibitor complex formation occurs in an immediate manner and a protease activity was discarded. The inhibition is non-competitive (Ki=1.5 × 10-6 M) without interactions among the binding sites. The complex is slightly dissociable and sucrose was able to partially reduce the inhibitory effect. Up to the present, invertase inhibitory proteins have been found solely in heterotrophic tissues. In this work we demonstrate that this protein is also present in an autotrophic tissue of a lower vascular plant.
Fil: Sayago, Jorge Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina
Fil: Vattuone, Marta Amelia. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Sampietro, A. R.. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina
Fil: Isla, Maria Ines. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Materia
Filicatae
Invertase Inhibitor Protein
Pteris Deflexa
Ptheridophyta
Β-D-Fructofuranoside Fructohydrolase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/62199
Acceder
id CONICETDig_fa4a45e67630307b9dc4efe108229e12
oai_identifier_str oai:ri.conicet.gov.ar:11336/62199
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling An invertase inhibitory protein from Pteris deflexa link frondsSayago, Jorge EstebanVattuone, Marta AmeliaSampietro, A. R.Isla, Maria InesFilicataeInvertase Inhibitor ProteinPteris DeflexaPtheridophytaΒ-D-Fructofuranoside Fructohydrolasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plant invertases play important roles in sucrose metabolism. Cell wall invertase was reported to participate in phloem loading and unloading. Soluble invertases would be involved in hexose level regulation in mature tissues and in stored sucrose utilization within vacuoles. Invertase inhibitory proteins were described as one of the possible mechanisms for invertase activity regulation in some plant species; nevertheless, these proteins were found only in sink tissues, suggesting that this mechanism would not be relevant in the sucrose turnover of leaves. This report describes the purification of invertase from Pteris deflexa fronds and the occurrence of an invertase inhibitory protein in this fern organ, as well as its purification and invertase-inhibitor interactions. The Mr of the invertase and of its inhibitory protein were 90,000 and 18,000, respectively. SDS-PAGE in the presence of 2-mercaptoetanol gave two subunits for the enzyme (Mr=66,000 and 30,000) and only one for the inhibitor. The inhibitor protein is a glycoprotein (12% w/w of neutral sugars) that did not show agglutinating activity like some others, and also showed a high heat stability at pH 5.0. The optimum pH of invertase activity is 5.0, while invertase inhibitory protein caused maximal inhibition at the same pH value. Invertase-inhibitor complex formation occurs in an immediate manner and a protease activity was discarded. The inhibition is non-competitive (Ki=1.5 × 10-6 M) without interactions among the binding sites. The complex is slightly dissociable and sucrose was able to partially reduce the inhibitory effect. Up to the present, invertase inhibitory proteins have been found solely in heterotrophic tissues. In this work we demonstrate that this protein is also present in an autotrophic tissue of a lower vascular plant.Fil: Sayago, Jorge Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; ArgentinaFil: Vattuone, Marta Amelia. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Sampietro, A. R.. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; ArgentinaFil: Isla, Maria Ines. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaTaylor & Francis2001-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/62199Sayago, Jorge Esteban; Vattuone, Marta Amelia; Sampietro, A. R.; Isla, Maria Ines; An invertase inhibitory protein from Pteris deflexa link fronds; Taylor & Francis; Journal Of Enzyme Inhibition; 16; 6; 12-2001; 517-5251475-63661475-6374CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1080/14756360127573info:eu-repo/semantics/altIdentifier/doi/10.1080/14756360127573info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:13:11Zoai:ri.conicet.gov.ar:11336/62199instacron: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 10:13:11.623CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv An invertase inhibitory protein from Pteris deflexa link fronds
title An invertase inhibitory protein from Pteris deflexa link fronds
spellingShingle An invertase inhibitory protein from Pteris deflexa link fronds
Sayago, Jorge Esteban
Filicatae
Invertase Inhibitor Protein
Pteris Deflexa
Ptheridophyta
Β-D-Fructofuranoside Fructohydrolase
title_short An invertase inhibitory protein from Pteris deflexa link fronds
title_full An invertase inhibitory protein from Pteris deflexa link fronds
title_fullStr An invertase inhibitory protein from Pteris deflexa link fronds
title_full_unstemmed An invertase inhibitory protein from Pteris deflexa link fronds
title_sort An invertase inhibitory protein from Pteris deflexa link fronds
dc.creator.none.fl_str_mv Sayago, Jorge Esteban
Vattuone, Marta Amelia
Sampietro, A. R.
Isla, Maria Ines
author Sayago, Jorge Esteban
author_facet Sayago, Jorge Esteban
Vattuone, Marta Amelia
Sampietro, A. R.
Isla, Maria Ines
author_role author
author2 Vattuone, Marta Amelia
Sampietro, A. R.
Isla, Maria Ines
author2_role author
author
author
dc.subject.none.fl_str_mv Filicatae
Invertase Inhibitor Protein
Pteris Deflexa
Ptheridophyta
Β-D-Fructofuranoside Fructohydrolase
topic Filicatae
Invertase Inhibitor Protein
Pteris Deflexa
Ptheridophyta
Β-D-Fructofuranoside Fructohydrolase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Plant invertases play important roles in sucrose metabolism. Cell wall invertase was reported to participate in phloem loading and unloading. Soluble invertases would be involved in hexose level regulation in mature tissues and in stored sucrose utilization within vacuoles. Invertase inhibitory proteins were described as one of the possible mechanisms for invertase activity regulation in some plant species; nevertheless, these proteins were found only in sink tissues, suggesting that this mechanism would not be relevant in the sucrose turnover of leaves. This report describes the purification of invertase from Pteris deflexa fronds and the occurrence of an invertase inhibitory protein in this fern organ, as well as its purification and invertase-inhibitor interactions. The Mr of the invertase and of its inhibitory protein were 90,000 and 18,000, respectively. SDS-PAGE in the presence of 2-mercaptoetanol gave two subunits for the enzyme (Mr=66,000 and 30,000) and only one for the inhibitor. The inhibitor protein is a glycoprotein (12% w/w of neutral sugars) that did not show agglutinating activity like some others, and also showed a high heat stability at pH 5.0. The optimum pH of invertase activity is 5.0, while invertase inhibitory protein caused maximal inhibition at the same pH value. Invertase-inhibitor complex formation occurs in an immediate manner and a protease activity was discarded. The inhibition is non-competitive (Ki=1.5 × 10-6 M) without interactions among the binding sites. The complex is slightly dissociable and sucrose was able to partially reduce the inhibitory effect. Up to the present, invertase inhibitory proteins have been found solely in heterotrophic tissues. In this work we demonstrate that this protein is also present in an autotrophic tissue of a lower vascular plant.
Fil: Sayago, Jorge Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina
Fil: Vattuone, Marta Amelia. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Sampietro, A. R.. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina
Fil: Isla, Maria Ines. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
description Plant invertases play important roles in sucrose metabolism. Cell wall invertase was reported to participate in phloem loading and unloading. Soluble invertases would be involved in hexose level regulation in mature tissues and in stored sucrose utilization within vacuoles. Invertase inhibitory proteins were described as one of the possible mechanisms for invertase activity regulation in some plant species; nevertheless, these proteins were found only in sink tissues, suggesting that this mechanism would not be relevant in the sucrose turnover of leaves. This report describes the purification of invertase from Pteris deflexa fronds and the occurrence of an invertase inhibitory protein in this fern organ, as well as its purification and invertase-inhibitor interactions. The Mr of the invertase and of its inhibitory protein were 90,000 and 18,000, respectively. SDS-PAGE in the presence of 2-mercaptoetanol gave two subunits for the enzyme (Mr=66,000 and 30,000) and only one for the inhibitor. The inhibitor protein is a glycoprotein (12% w/w of neutral sugars) that did not show agglutinating activity like some others, and also showed a high heat stability at pH 5.0. The optimum pH of invertase activity is 5.0, while invertase inhibitory protein caused maximal inhibition at the same pH value. Invertase-inhibitor complex formation occurs in an immediate manner and a protease activity was discarded. The inhibition is non-competitive (Ki=1.5 × 10-6 M) without interactions among the binding sites. The complex is slightly dissociable and sucrose was able to partially reduce the inhibitory effect. Up to the present, invertase inhibitory proteins have been found solely in heterotrophic tissues. In this work we demonstrate that this protein is also present in an autotrophic tissue of a lower vascular plant.
publishDate 2001
dc.date.none.fl_str_mv 2001-12
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/11336/62199
Sayago, Jorge Esteban; Vattuone, Marta Amelia; Sampietro, A. R.; Isla, Maria Ines; An invertase inhibitory protein from Pteris deflexa link fronds; Taylor & Francis; Journal Of Enzyme Inhibition; 16; 6; 12-2001; 517-525
1475-6366
1475-6374
CONICET Digital
CONICET
url http://hdl.handle.net/11336/62199
identifier_str_mv Sayago, Jorge Esteban; Vattuone, Marta Amelia; Sampietro, A. R.; Isla, Maria Ines; An invertase inhibitory protein from Pteris deflexa link fronds; Taylor & Francis; Journal Of Enzyme Inhibition; 16; 6; 12-2001; 517-525
1475-6366
1475-6374
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1080/14756360127573
info:eu-repo/semantics/altIdentifier/doi/10.1080/14756360127573
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
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
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score 13.070432

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