Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity

Autores
Sayago, Jorge Esteban; Vattuone, Marta Amelia; Sampiettro, A. R.; Isla, Maria Ines
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
An acid invertase from the fern Pteris deflexa Link was purified and the effect of reaction products on enzyme activity was studied. Fructose and glucose were competitive and non-competitive inhibitors of the enzyme, respectively. Since proteins suppressed glucose and fructose inhibition of the enzyme, an invertase modulation by reaction products is unlikely; nevertheless, an invertase proteinaceous inhibitor previously reported could have a role in this respect. The purified enzyme was an heterodimer Mr 90,000 Daltons composed of subunits of 66,000 and 30,000 Daltons. The enzyme had β-fructofuranosidase activity and hydrolyzed mainly sucrose but also raffinose and stachyose, with Km of 3.22, 10.80 and 38.50 mM, respectively. Invertase activity with an optimum pH at 5.0 was present in almost every leaf fern tissue. Pinnas (sporophyll leaflets) had the higher enzyme levels. Invertase histochemical and immunochemical localization studies showed the enzyme mainly in phloem cells. Epidermis, collenchyma and parenchyma cells also showed invertase protein.
Fil: Sayago, Jorge Esteban. 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; Argentina
Fil: Sampiettro, 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
Β-D-Fructofuranoside Fructohydrolase
Fructose
Proteinaceous Inhibitor
Pteris Deflexa Link
Soluble Acid Invertase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/62223
Acceder
id CONICETDig_8144b2d584ecae3dd00e8130800fba81
oai_identifier_str oai:ri.conicet.gov.ar:11336/62223
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activitySayago, Jorge EstebanVattuone, Marta AmeliaSampiettro, A. R.Isla, Maria InesΒ-D-Fructofuranoside FructohydrolaseFructoseProteinaceous InhibitorPteris Deflexa LinkSoluble Acid Invertasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1An acid invertase from the fern Pteris deflexa Link was purified and the effect of reaction products on enzyme activity was studied. Fructose and glucose were competitive and non-competitive inhibitors of the enzyme, respectively. Since proteins suppressed glucose and fructose inhibition of the enzyme, an invertase modulation by reaction products is unlikely; nevertheless, an invertase proteinaceous inhibitor previously reported could have a role in this respect. The purified enzyme was an heterodimer Mr 90,000 Daltons composed of subunits of 66,000 and 30,000 Daltons. The enzyme had β-fructofuranosidase activity and hydrolyzed mainly sucrose but also raffinose and stachyose, with Km of 3.22, 10.80 and 38.50 mM, respectively. Invertase activity with an optimum pH at 5.0 was present in almost every leaf fern tissue. Pinnas (sporophyll leaflets) had the higher enzyme levels. Invertase histochemical and immunochemical localization studies showed the enzyme mainly in phloem cells. Epidermis, collenchyma and parenchyma cells also showed invertase protein.Fil: Sayago, Jorge Esteban. 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; ArgentinaFil: Sampiettro, 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 & Francis Ltd2002-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/62223Sayago, Jorge Esteban; Vattuone, Marta Amelia; Sampiettro, A. R.; Isla, Maria Ines; Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity; Taylor & Francis Ltd; Journal of Enzyme Inhibition and Medicinal Chemistry; 17; 2; 12-2002; 123-1308755-5093CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1080/14756360290026450info:eu-repo/semantics/altIdentifier/doi/10.1080/14756360290026450info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:44:08Zoai:ri.conicet.gov.ar:11336/62223instacron: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 10:44:08.774CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity
title Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity
spellingShingle Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity
Sayago, Jorge Esteban
Β-D-Fructofuranoside Fructohydrolase
Fructose
Proteinaceous Inhibitor
Pteris Deflexa Link
Soluble Acid Invertase
title_short Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity
title_full Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity
title_fullStr Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity
title_full_unstemmed Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity
title_sort Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity
dc.creator.none.fl_str_mv Sayago, Jorge Esteban
Vattuone, Marta Amelia
Sampiettro, A. R.
Isla, Maria Ines
author Sayago, Jorge Esteban
author_facet Sayago, Jorge Esteban
Vattuone, Marta Amelia
Sampiettro, A. R.
Isla, Maria Ines
author_role author
author2 Vattuone, Marta Amelia
Sampiettro, A. R.
Isla, Maria Ines
author2_role author
author
author
dc.subject.none.fl_str_mv Β-D-Fructofuranoside Fructohydrolase
Fructose
Proteinaceous Inhibitor
Pteris Deflexa Link
Soluble Acid Invertase
topic Β-D-Fructofuranoside Fructohydrolase
Fructose
Proteinaceous Inhibitor
Pteris Deflexa Link
Soluble Acid Invertase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv An acid invertase from the fern Pteris deflexa Link was purified and the effect of reaction products on enzyme activity was studied. Fructose and glucose were competitive and non-competitive inhibitors of the enzyme, respectively. Since proteins suppressed glucose and fructose inhibition of the enzyme, an invertase modulation by reaction products is unlikely; nevertheless, an invertase proteinaceous inhibitor previously reported could have a role in this respect. The purified enzyme was an heterodimer Mr 90,000 Daltons composed of subunits of 66,000 and 30,000 Daltons. The enzyme had β-fructofuranosidase activity and hydrolyzed mainly sucrose but also raffinose and stachyose, with Km of 3.22, 10.80 and 38.50 mM, respectively. Invertase activity with an optimum pH at 5.0 was present in almost every leaf fern tissue. Pinnas (sporophyll leaflets) had the higher enzyme levels. Invertase histochemical and immunochemical localization studies showed the enzyme mainly in phloem cells. Epidermis, collenchyma and parenchyma cells also showed invertase protein.
Fil: Sayago, Jorge Esteban. 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; Argentina
Fil: Sampiettro, 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 An acid invertase from the fern Pteris deflexa Link was purified and the effect of reaction products on enzyme activity was studied. Fructose and glucose were competitive and non-competitive inhibitors of the enzyme, respectively. Since proteins suppressed glucose and fructose inhibition of the enzyme, an invertase modulation by reaction products is unlikely; nevertheless, an invertase proteinaceous inhibitor previously reported could have a role in this respect. The purified enzyme was an heterodimer Mr 90,000 Daltons composed of subunits of 66,000 and 30,000 Daltons. The enzyme had β-fructofuranosidase activity and hydrolyzed mainly sucrose but also raffinose and stachyose, with Km of 3.22, 10.80 and 38.50 mM, respectively. Invertase activity with an optimum pH at 5.0 was present in almost every leaf fern tissue. Pinnas (sporophyll leaflets) had the higher enzyme levels. Invertase histochemical and immunochemical localization studies showed the enzyme mainly in phloem cells. Epidermis, collenchyma and parenchyma cells also showed invertase protein.
publishDate 2002
dc.date.none.fl_str_mv 2002-12
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/11336/62223
Sayago, Jorge Esteban; Vattuone, Marta Amelia; Sampiettro, A. R.; Isla, Maria Ines; Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity; Taylor & Francis Ltd; Journal of Enzyme Inhibition and Medicinal Chemistry; 17; 2; 12-2002; 123-130
8755-5093
CONICET Digital
CONICET
url http://hdl.handle.net/11336/62223
identifier_str_mv Sayago, Jorge Esteban; Vattuone, Marta Amelia; Sampiettro, A. R.; Isla, Maria Ines; Proteinaceous inhibitor versus fructose as modulators of Pteris deflexa invertase activity; Taylor & Francis Ltd; Journal of Enzyme Inhibition and Medicinal Chemistry; 17; 2; 12-2002; 123-130
8755-5093
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/10.1080/14756360290026450
info:eu-repo/semantics/altIdentifier/doi/10.1080/14756360290026450
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Taylor & Francis Ltd
publisher.none.fl_str_mv Taylor & Francis Ltd
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_ 1844614477980368896
score 13.070432

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