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dc.contributor.author
Sayago, Jorge Esteban
dc.contributor.author
Vattuone, Marta Amelia
dc.contributor.author
Sampietro, A. R.
dc.contributor.author
Isla, Maria Ines
dc.date.available
2018-10-11T16:04:52Z
dc.date.issued
2001-12
dc.identifier.citation
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
dc.identifier.issn
1475-6366
dc.identifier.uri
http://hdl.handle.net/11336/62199
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Taylor & Francis
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.subject
Filicatae
dc.subject
Invertase Inhibitor Protein
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Pteris Deflexa
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Ptheridophyta
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Β-D-Fructofuranoside Fructohydrolase
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
An invertase inhibitory protein from Pteris deflexa link fronds
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-10-09T20:32:35Z
dc.identifier.eissn
1475-6374
dc.journal.volume
16
dc.journal.number
6
dc.journal.pagination
517-525
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Filadelfia
dc.description.fil
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
dc.description.fil
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
dc.description.fil
Fil: Sampietro, A. R.. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Estudios Vegetales; Argentina
dc.description.fil
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
dc.journal.title
Journal Of Enzyme Inhibition
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1080/14756360127573
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1080/14756360127573
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