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

Mostrar todas las versiones(3)

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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Rossetti, M.V., de Geralnik, A.A.J., Kotler, M., Fumagalli, S., del C. Batlle, A.M.
Formato:	Artículo publishedVersion
Lenguaje:	Inglés
Publicado:	1980
Materias:	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 Isomerases Liver Macromolecular Systems Molecular Weight Multienzyme Complexes Plants Protein Conformation Species Specificity Support, Non-U.S. Gov't
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p761_Rossetti
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paperaa:paper_0020711X_v12_n5-6_p761_Rossetti
record_format	dspace
spelling	paperaa:paper_0020711X_v12_n5-6_p761_Rossetti2023-06-12T16:42:08Z 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 Int. J. Biochem. 1980;12(5-6):761-767 Rossetti, M.V. de Geralnik, A.A.J. Kotler, M. Fumagalli, S. del C. Batlle, A.M. 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 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. 1980 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p761_Rossetti
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language	Inglés
orig_language_str_mv	eng
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
spellingShingle	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 Rossetti, M.V. de Geralnik, A.A.J. Kotler, M. Fumagalli, S. del C. Batlle, A.M. 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
topic_facet	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
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.
format	Artículo Artículo publishedVersion
author	Rossetti, M.V. de Geralnik, A.A.J. Kotler, M. Fumagalli, S. del C. Batlle, A.M.
author_facet	Rossetti, M.V. de Geralnik, A.A.J. Kotler, M. Fumagalli, S. del C. Batlle, A.M.
author_sort	Rossetti, M.V.
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
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
publishDate	1980
url	http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p761_Rossetti
work_keys_str_mv	AT rossettimv occurrenceofmultiplemolecularformsofporphobilinogenaseindiverseorganismstheminimumquaternarystructureofporphobilinogenaseisaprotomerofonedeaminaseandoneisomerasedomain AT degeralnikaaj occurrenceofmultiplemolecularformsofporphobilinogenaseindiverseorganismstheminimumquaternarystructureofporphobilinogenaseisaprotomerofonedeaminaseandoneisomerasedomain AT kotlerm occurrenceofmultiplemolecularformsofporphobilinogenaseindiverseorganismstheminimumquaternarystructureofporphobilinogenaseisaprotomerofonedeaminaseandoneisomerasedomain AT fumagallis occurrenceofmultiplemolecularformsofporphobilinogenaseindiverseorganismstheminimumquaternarystructureofporphobilinogenaseisaprotomerofonedeaminaseandoneisomerasedomain AT delcbatlleam occurrenceofmultiplemolecularformsofporphobilinogenaseindiverseorganismstheminimumquaternarystructureofporphobilinogenaseisaprotomerofonedeaminaseandoneisomerasedomain
_version_	1769810372106125312

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

Ejemplares similares