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
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...
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1980
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p761_Rossetti http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p761_Rossetti |
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paper:paper_0020711X_v12_n5-6_p761_Rossetti2023-06-08T14:41:03Z 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, María Victoria Kotler, Mónica Lidia Fumagalli, Silvia Ana Batlle, Alcira María del Carmen 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 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p761_Rossetti 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) |
| 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, María Victoria Kotler, Mónica Lidia Fumagalli, Silvia Ana Batlle, Alcira María del Carmen 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. |
| author |
Rossetti, María Victoria Kotler, Mónica Lidia Fumagalli, Silvia Ana Batlle, Alcira María del Carmen |
| author_facet |
Rossetti, María Victoria Kotler, Mónica Lidia Fumagalli, Silvia Ana Batlle, Alcira María del Carmen |
| author_sort |
Rossetti, María Victoria |
| 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 |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p761_Rossetti http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p761_Rossetti |
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| _version_ |
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