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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_0020711X_v12_n5-6_p757_Stafforini
Ver los metadatos del registro completo
id |
BDUBAFCEN_0f08913d5eb7647a4385e2c7713dd56b |
---|---|
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 |
_version_ |
1844618732836487169 |
score |
13.070432 |