Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one iso...

Autores: Rossetti, M.V.; de Geralnik, A.A.J.; Kotler, M.; Fumagalli, S.; del C. Batlle, A.M.
Año de publicación: 1980
Idioma: inglés
Tipo de recurso: artículo
Estado: versión publicada
Descripción: 1. 1. Gel filtration on Sephadex G-100 and Sepharose 4B were used to redetermine the molecular weight (MW) of porphobilinogenase, deaminase and isomerase purified from different sources, and determine the MW of these enzymes purified from Eugtena gracilis. 2. 2. Results reported here, indicate that porphobilinogenase can be found, into three different molecular forms, tetramers, dimers and monomers according to the source organism. 3. 3. It is proposed that minimal functional structure of PBGase is a hybrid protomer of MW 25,000, composed by two different domains, in a ratio of 1 mol of deaminase, MW 20,000 to 1 mol of isomerase. MW 5000. 4. 4. A model explaining the occurrence of different MW species of PBGase in nature and the possible interconversion among the various forms is postulated. © 1980.
Fil:Rossetti, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Kotler, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Fumagalli, S. 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):761-767
Materia: ammonia lyase
Ammonia Lyases
hydrolase
isomerase
multienzyme complex
animal
article
bird
cattle
comparative study
enzymology
erythrocyte
Euglena gracilis
isolation and purification
liver
macromolecule
molecular weight
plant
protein conformation
species difference
Aminohydrolases
Ammonia-Lyases
Animal
Birds
Cattle
Comparative Study
Erythrocytes
Euglena gracilis
Isomerases
Liver
Macromolecular Systems
Molecular Weight
Multienzyme Complexes
Plants
Protein Conformation
Species Specificity
Support, Non-U.S. Gov't
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_p761_Rossetti

Acceder

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network_acronym_str	BDUBAFCEN
repository_id_str	1896
network_name_str	Biblioteca Digital (UBA-FCEN)
spelling	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domainRossetti, M.V.de Geralnik, A.A.J.Kotler, M.Fumagalli, S.del C. Batlle, A.M.ammonia lyaseAmmonia Lyaseshydrolaseisomerasemultienzyme complexanimalarticlebirdcattlecomparative studyenzymologyerythrocyteEuglena gracilisisolation and purificationlivermacromoleculemolecular weightplantprotein conformationspecies differenceAminohydrolasesAmmonia-LyasesAnimalBirdsCattleComparative StudyErythrocytesEuglena gracilisIsomerasesLiverMacromolecular SystemsMolecular WeightMultienzyme ComplexesPlantsProtein ConformationSpecies SpecificitySupport, Non-U.S. Gov't1. 1. Gel filtration on Sephadex G-100 and Sepharose 4B were used to redetermine the molecular weight (MW) of porphobilinogenase, deaminase and isomerase purified from different sources, and determine the MW of these enzymes purified from Eugtena gracilis. 2. 2. Results reported here, indicate that porphobilinogenase can be found, into three different molecular forms, tetramers, dimers and monomers according to the source organism. 3. 3. It is proposed that minimal functional structure of PBGase is a hybrid protomer of MW 25,000, composed by two different domains, in a ratio of 1 mol of deaminase, MW 20,000 to 1 mol of isomerase. MW 5000. 4. 4. A model explaining the occurrence of different MW species of PBGase in nature and the possible interconversion among the various forms is postulated. © 1980.Fil:Rossetti, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Kotler, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Fumagalli, S. 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_p761_RossettiInt. J. Biochem. 1980;12(5-6):761-767reponame: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/ar2025-09-29T13:43:09Zpaperaa:paper_0020711X_v12_n5-6_p761_RossettiInstitucionalhttps://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 13:43:10.53Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain
title	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain
spellingShingle	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain Rossetti, M.V. ammonia lyase Ammonia Lyases hydrolase isomerase multienzyme complex animal article bird cattle comparative study enzymology erythrocyte Euglena gracilis isolation and purification liver macromolecule molecular weight plant protein conformation species difference Aminohydrolases Ammonia-Lyases Animal Birds Cattle Comparative Study Erythrocytes Euglena gracilis Isomerases Liver Macromolecular Systems Molecular Weight Multienzyme Complexes Plants Protein Conformation Species Specificity Support, Non-U.S. Gov't
title_short	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain
title_full	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain
title_fullStr	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain
title_full_unstemmed	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain
title_sort	Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain
dc.creator.none.fl_str_mv	Rossetti, M.V. de Geralnik, A.A.J. Kotler, M. Fumagalli, S. del C. Batlle, A.M.
author	Rossetti, M.V.
author_facet	Rossetti, M.V. de Geralnik, A.A.J. Kotler, M. Fumagalli, S. del C. Batlle, A.M.
author_role	author
author2	de Geralnik, A.A.J. Kotler, M. Fumagalli, S. del C. Batlle, A.M.
author2_role	author author author author
dc.subject.none.fl_str_mv	ammonia lyase Ammonia Lyases hydrolase isomerase multienzyme complex animal article bird cattle comparative study enzymology erythrocyte Euglena gracilis isolation and purification liver macromolecule molecular weight plant protein conformation species difference Aminohydrolases Ammonia-Lyases Animal Birds Cattle Comparative Study Erythrocytes Euglena gracilis Isomerases Liver Macromolecular Systems Molecular Weight Multienzyme Complexes Plants Protein Conformation Species Specificity Support, Non-U.S. Gov't
topic	ammonia lyase Ammonia Lyases hydrolase isomerase multienzyme complex animal article bird cattle comparative study enzymology erythrocyte Euglena gracilis isolation and purification liver macromolecule molecular weight plant protein conformation species difference Aminohydrolases Ammonia-Lyases Animal Birds Cattle Comparative Study Erythrocytes Euglena gracilis Isomerases Liver Macromolecular Systems Molecular Weight Multienzyme Complexes Plants Protein Conformation Species Specificity Support, Non-U.S. Gov't
dc.description.none.fl_txt_mv	1. 1. Gel filtration on Sephadex G-100 and Sepharose 4B were used to redetermine the molecular weight (MW) of porphobilinogenase, deaminase and isomerase purified from different sources, and determine the MW of these enzymes purified from Eugtena gracilis. 2. 2. Results reported here, indicate that porphobilinogenase can be found, into three different molecular forms, tetramers, dimers and monomers according to the source organism. 3. 3. It is proposed that minimal functional structure of PBGase is a hybrid protomer of MW 25,000, composed by two different domains, in a ratio of 1 mol of deaminase, MW 20,000 to 1 mol of isomerase. MW 5000. 4. 4. A model explaining the occurrence of different MW species of PBGase in nature and the possible interconversion among the various forms is postulated. © 1980. Fil:Rossetti, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kotler, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Fumagalli, S. 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. Gel filtration on Sephadex G-100 and Sepharose 4B were used to redetermine the molecular weight (MW) of porphobilinogenase, deaminase and isomerase purified from different sources, and determine the MW of these enzymes purified from Eugtena gracilis. 2. 2. Results reported here, indicate that porphobilinogenase can be found, into three different molecular forms, tetramers, dimers and monomers according to the source organism. 3. 3. It is proposed that minimal functional structure of PBGase is a hybrid protomer of MW 25,000, composed by two different domains, in a ratio of 1 mol of deaminase, MW 20,000 to 1 mol of isomerase. MW 5000. 4. 4. A model explaining the occurrence of different MW species of PBGase in nature and the possible interconversion among the various forms is postulated. © 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_p761_Rossetti
url	http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p761_Rossetti
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):761-767 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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Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: The minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one iso...

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