Influencing its molecular weight determination

Autores
Stafforini, D.M.; Polo, C.F.; Stella, A.M.; De Xifra, E.W.; Del C. Batlle, A.M.
Año de publicación
1980
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
1. 1. By chromatography through Sephadex G-200 of increasing amounts of partially purified pig liver ALA-D, different profiles were obtained, showing that species of molecular weights ranging from 140,000 to 560,000 might exist in equilibrium, but their relative ratio was dependent on the total amount of protein sampled. In all cases, however, the main peak (60-70%) corresponded to the 280,000 MW oligomer, that is the octamer. 2. 2. It was found that elution profiles were also dependent on column dimensions and on the purity of the enzyme preparation. 3. 3. K+ ions affected both catalytic activity and aggregation of the enzyme. 4. Results here reported add further support to the proposal of the existence of a minimal functional dimer. © 1980.
Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Int. J. Biochem. 1980;12(5-6):757-760
Materia
porphobilinogen synthase
potassium
animal
article
enzymology
isolation and purification
liver
macromolecule
metabolism
molecular weight
swine
Animal
Liver
Macromolecular Systems
Molecular Weight
Porphobilinogen Synthase
Potassium
Support, Non-U.S. Gov't
Swine
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_0020711X_v12_n5-6_p757_Stafforini

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oai_identifier_str paperaa:paper_0020711X_v12_n5-6_p757_Stafforini
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Influencing its molecular weight determinationStafforini, D.M.Polo, C.F.Stella, A.M.De Xifra, E.W.Del C. Batlle, A.M.porphobilinogen synthasepotassiumanimalarticleenzymologyisolation and purificationlivermacromoleculemetabolismmolecular weightswineAnimalLiverMacromolecular SystemsMolecular WeightPorphobilinogen SynthasePotassiumSupport, Non-U.S. Gov'tSwine1. 1. By chromatography through Sephadex G-200 of increasing amounts of partially purified pig liver ALA-D, different profiles were obtained, showing that species of molecular weights ranging from 140,000 to 560,000 might exist in equilibrium, but their relative ratio was dependent on the total amount of protein sampled. In all cases, however, the main peak (60-70%) corresponded to the 280,000 MW oligomer, that is the octamer. 2. 2. It was found that elution profiles were also dependent on column dimensions and on the purity of the enzyme preparation. 3. 3. K+ ions affected both catalytic activity and aggregation of the enzyme. 4. Results here reported add further support to the proposal of the existence of a minimal functional dimer. © 1980.Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1980info: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_0020711X_v12_n5-6_p757_StafforiniInt. J. Biochem. 1980;12(5-6):757-760reponame: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/ar2025-09-29T13:42:49Zpaperaa:paper_0020711X_v12_n5-6_p757_StafforiniInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:42:50.568Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Influencing its molecular weight determination
title Influencing its molecular weight determination
spellingShingle Influencing its molecular weight determination
Stafforini, D.M.
porphobilinogen synthase
potassium
animal
article
enzymology
isolation and purification
liver
macromolecule
metabolism
molecular weight
swine
Animal
Liver
Macromolecular Systems
Molecular Weight
Porphobilinogen Synthase
Potassium
Support, Non-U.S. Gov't
Swine
title_short Influencing its molecular weight determination
title_full Influencing its molecular weight determination
title_fullStr Influencing its molecular weight determination
title_full_unstemmed Influencing its molecular weight determination
title_sort Influencing its molecular weight determination
dc.creator.none.fl_str_mv Stafforini, D.M.
Polo, C.F.
Stella, A.M.
De Xifra, E.W.
Del C. Batlle, A.M.
author Stafforini, D.M.
author_facet Stafforini, D.M.
Polo, C.F.
Stella, A.M.
De Xifra, E.W.
Del C. Batlle, A.M.
author_role author
author2 Polo, C.F.
Stella, A.M.
De Xifra, E.W.
Del C. Batlle, A.M.
author2_role author
author
author
author
dc.subject.none.fl_str_mv porphobilinogen synthase
potassium
animal
article
enzymology
isolation and purification
liver
macromolecule
metabolism
molecular weight
swine
Animal
Liver
Macromolecular Systems
Molecular Weight
Porphobilinogen Synthase
Potassium
Support, Non-U.S. Gov't
Swine
topic porphobilinogen synthase
potassium
animal
article
enzymology
isolation and purification
liver
macromolecule
metabolism
molecular weight
swine
Animal
Liver
Macromolecular Systems
Molecular Weight
Porphobilinogen Synthase
Potassium
Support, Non-U.S. Gov't
Swine
dc.description.none.fl_txt_mv 1. 1. By chromatography through Sephadex G-200 of increasing amounts of partially purified pig liver ALA-D, different profiles were obtained, showing that species of molecular weights ranging from 140,000 to 560,000 might exist in equilibrium, but their relative ratio was dependent on the total amount of protein sampled. In all cases, however, the main peak (60-70%) corresponded to the 280,000 MW oligomer, that is the octamer. 2. 2. It was found that elution profiles were also dependent on column dimensions and on the purity of the enzyme preparation. 3. 3. K+ ions affected both catalytic activity and aggregation of the enzyme. 4. Results here reported add further support to the proposal of the existence of a minimal functional dimer. © 1980.
Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description 1. 1. By chromatography through Sephadex G-200 of increasing amounts of partially purified pig liver ALA-D, different profiles were obtained, showing that species of molecular weights ranging from 140,000 to 560,000 might exist in equilibrium, but their relative ratio was dependent on the total amount of protein sampled. In all cases, however, the main peak (60-70%) corresponded to the 280,000 MW oligomer, that is the octamer. 2. 2. It was found that elution profiles were also dependent on column dimensions and on the purity of the enzyme preparation. 3. 3. K+ ions affected both catalytic activity and aggregation of the enzyme. 4. Results here reported add further support to the proposal of the existence of a minimal functional dimer. © 1980.
publishDate 1980
dc.date.none.fl_str_mv 1980
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_0020711X_v12_n5-6_p757_Stafforini
url http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p757_Stafforini
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 Int. J. Biochem. 1980;12(5-6):757-760
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 13.070432