Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid supp...

Autores
de Xifra, E.A.W.; Mendiara, S.; del C. Batlle, A.M.
Año de publicación
1972
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
FEBS Lett. 1972;27(2):275-278
Materia
adenosine triphosphate
long chain fatty acid coenzyme A ligase
polysaccharide
succinic acid derivative
affinity chromatography
article
binding site
enzymology
kinetics
macromolecule
metabolism
plant
protein binding
Adenosine Triphosphate
Binding Sites
Chromatography, Affinity
Coenzyme A Ligases
Kinetics
Macromolecular Systems
Plants
Polysaccharides
Protein Binding
Succinates
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00145793_v27_n2_p275_deXifra
Acceder
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oai_identifier_str paperaa:paper_00145793_v27_n2_p275_deXifra
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid supportde Xifra, E.A.W.Mendiara, S.del C. Batlle, A.M.adenosine triphosphatelong chain fatty acid coenzyme A ligasepolysaccharidesuccinic acid derivativeaffinity chromatographyarticlebinding siteenzymologykineticsmacromoleculemetabolismplantprotein bindingAdenosine TriphosphateBinding SitesChromatography, AffinityCoenzyme A LigasesKineticsMacromolecular SystemsPlantsPolysaccharidesProtein BindingSuccinatesFil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1972info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00145793_v27_n2_p275_deXifraFEBS Lett. 1972;27(2):275-278reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-10-23T11:18:18Zpaperaa:paper_00145793_v27_n2_p275_deXifraInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-23 11:18:20.006Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
spellingShingle Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
de Xifra, E.A.W.
adenosine triphosphate
long chain fatty acid coenzyme A ligase
polysaccharide
succinic acid derivative
affinity chromatography
article
binding site
enzymology
kinetics
macromolecule
metabolism
plant
protein binding
Adenosine Triphosphate
Binding Sites
Chromatography, Affinity
Coenzyme A Ligases
Kinetics
Macromolecular Systems
Plants
Polysaccharides
Protein Binding
Succinates
title_short Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_full Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_fullStr Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_full_unstemmed Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_sort Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
dc.creator.none.fl_str_mv de Xifra, E.A.W.
Mendiara, S.
del C. Batlle, A.M.
author de Xifra, E.A.W.
author_facet de Xifra, E.A.W.
Mendiara, S.
del C. Batlle, A.M.
author_role author
author2 Mendiara, S.
del C. Batlle, A.M.
author2_role author
author
dc.subject.none.fl_str_mv adenosine triphosphate
long chain fatty acid coenzyme A ligase
polysaccharide
succinic acid derivative
affinity chromatography
article
binding site
enzymology
kinetics
macromolecule
metabolism
plant
protein binding
Adenosine Triphosphate
Binding Sites
Chromatography, Affinity
Coenzyme A Ligases
Kinetics
Macromolecular Systems
Plants
Polysaccharides
Protein Binding
Succinates
topic adenosine triphosphate
long chain fatty acid coenzyme A ligase
polysaccharide
succinic acid derivative
affinity chromatography
article
binding site
enzymology
kinetics
macromolecule
metabolism
plant
protein binding
Adenosine Triphosphate
Binding Sites
Chromatography, Affinity
Coenzyme A Ligases
Kinetics
Macromolecular Systems
Plants
Polysaccharides
Protein Binding
Succinates
dc.description.none.fl_txt_mv Fil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Fil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
publishDate 1972
dc.date.none.fl_str_mv 1972
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/20.500.12110/paper_00145793_v27_n2_p275_deXifra
url http://hdl.handle.net/20.500.12110/paper_00145793_v27_n2_p275_deXifra
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv FEBS Lett. 1972;27(2):275-278
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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score 12.982451

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