Influencing its molecular weight determination
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 amou...
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| Formato: | Artículo publishedVersion |
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1980
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p757_Stafforini http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v12_n5-6_p757_Stafforini_oai |
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I28-R145-paper_0020711X_v12_n5-6_p757_Stafforini_oai2020-10-19 Stafforini, D.M. Polo, C.F. Stella, A.M. De Xifra, E.W. Del C. Batlle, A.M. 1980 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. application/pdf http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p757_Stafforini info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Int. J. Biochem. 1980;12(5-6):757-760 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 Influencing its molecular weight determination info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v12_n5-6_p757_Stafforini_oai |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-145 |
| collection |
Repositorio Digital de la Universidad de Buenos Aires (UBA) |
| 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 |
| spellingShingle |
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 Stafforini, D.M. Polo, C.F. Stella, A.M. De Xifra, E.W. Del C. Batlle, A.M. Influencing its molecular weight determination |
| topic_facet |
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 |
| 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. |
| format |
Artículo Artículo publishedVersion |
| author |
Stafforini, D.M. Polo, C.F. Stella, A.M. De Xifra, E.W. Del C. Batlle, A.M. |
| author_facet |
Stafforini, D.M. Polo, C.F. Stella, A.M. De Xifra, E.W. Del C. Batlle, A.M. |
| author_sort |
Stafforini, D.M. |
| title |
Influencing its molecular weight determination |
| 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 |
| publishDate |
1980 |
| url |
http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p757_Stafforini http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v12_n5-6_p757_Stafforini_oai |
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AT stafforinidm influencingitsmolecularweightdetermination AT polocf influencingitsmolecularweightdetermination AT stellaam influencingitsmolecularweightdetermination AT dexifraew influencingitsmolecularweightdetermination AT delcbatlleam influencingitsmolecularweightdetermination |
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