Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris
Rhodopseudomonas palustris uroporphyrinogen I synthetase (URO‐S) has been chemically attached to Sepharose 4B and some of its properties have been studied. When 7–8 mg protein/ml activated Sepharose was used, immobilized URO‐S retained 45% of the activity of the original soluble preparation, with a...
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1990
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08854513_v12_n3_p252_Kotler http://hdl.handle.net/20.500.12110/paper_08854513_v12_n3_p252_Kotler |
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paper:paper_08854513_v12_n3_p252_Kotler2023-06-08T15:46:41Z Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris Kotler, Mónica Lidia Juknat, Adela Ana Batlle, Alcira María del Carmen porphyrinogen synthetase uroporphyrin article enzyme immobilization nonhuman rhodopseudomonas palustris Ammonia-Lyases Biotechnology Enzymes, Immobilized Heat Hydrogen-Ion Concentration Hydroxymethylbilane Synthase Kinetics Rhodopseudomonas Sepharose Support, Non-U.S. Gov't Rhodopseudomonas palustris Rhodopseudomonas palustris uroporphyrinogen I synthetase (URO‐S) has been chemically attached to Sepharose 4B and some of its properties have been studied. When 7–8 mg protein/ml activated Sepharose was used, immobilized URO‐S retained 45% of the activity of the original soluble preparation, with a coupling yield of 66% after a period of 15 h. Optimal incubation conditions for the activity of gel‐enzyme were determined. Unlike the soluble enzyme, the Sepharose‐bound URO‐S showed a biphasic substrate saturation curve, indicating that a protein conformational change had occurred during the process of immobilization. Immobilized URO‐S stored at 4 degrees C for 35 days retained 90% of activity and when repeatedly used, up to 5 times, retained 48% of the original activity. Attachment of URO‐S to Sepharose led to an enhanced thermal stability. 1990 The Swiss Political Science Review Fil:Kotler, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Juknat, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A.M.D.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1990 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08854513_v12_n3_p252_Kotler http://hdl.handle.net/20.500.12110/paper_08854513_v12_n3_p252_Kotler |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
porphyrinogen synthetase uroporphyrin article enzyme immobilization nonhuman rhodopseudomonas palustris Ammonia-Lyases Biotechnology Enzymes, Immobilized Heat Hydrogen-Ion Concentration Hydroxymethylbilane Synthase Kinetics Rhodopseudomonas Sepharose Support, Non-U.S. Gov't Rhodopseudomonas palustris |
| spellingShingle |
porphyrinogen synthetase uroporphyrin article enzyme immobilization nonhuman rhodopseudomonas palustris Ammonia-Lyases Biotechnology Enzymes, Immobilized Heat Hydrogen-Ion Concentration Hydroxymethylbilane Synthase Kinetics Rhodopseudomonas Sepharose Support, Non-U.S. Gov't Rhodopseudomonas palustris Kotler, Mónica Lidia Juknat, Adela Ana Batlle, Alcira María del Carmen Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris |
| topic_facet |
porphyrinogen synthetase uroporphyrin article enzyme immobilization nonhuman rhodopseudomonas palustris Ammonia-Lyases Biotechnology Enzymes, Immobilized Heat Hydrogen-Ion Concentration Hydroxymethylbilane Synthase Kinetics Rhodopseudomonas Sepharose Support, Non-U.S. Gov't Rhodopseudomonas palustris |
| description |
Rhodopseudomonas palustris uroporphyrinogen I synthetase (URO‐S) has been chemically attached to Sepharose 4B and some of its properties have been studied. When 7–8 mg protein/ml activated Sepharose was used, immobilized URO‐S retained 45% of the activity of the original soluble preparation, with a coupling yield of 66% after a period of 15 h. Optimal incubation conditions for the activity of gel‐enzyme were determined. Unlike the soluble enzyme, the Sepharose‐bound URO‐S showed a biphasic substrate saturation curve, indicating that a protein conformational change had occurred during the process of immobilization. Immobilized URO‐S stored at 4 degrees C for 35 days retained 90% of activity and when repeatedly used, up to 5 times, retained 48% of the original activity. Attachment of URO‐S to Sepharose led to an enhanced thermal stability. 1990 The Swiss Political Science Review |
| author |
Kotler, Mónica Lidia Juknat, Adela Ana Batlle, Alcira María del Carmen |
| author_facet |
Kotler, Mónica Lidia Juknat, Adela Ana Batlle, Alcira María del Carmen |
| author_sort |
Kotler, Mónica Lidia |
| title |
Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris |
| title_short |
Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris |
| title_full |
Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris |
| title_fullStr |
Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris |
| title_full_unstemmed |
Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris |
| title_sort |
immobilized uroporphyrinogen i synthetase from rhodopseudomonas palustris |
| publishDate |
1990 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08854513_v12_n3_p252_Kotler http://hdl.handle.net/20.500.12110/paper_08854513_v12_n3_p252_Kotler |
| work_keys_str_mv |
AT kotlermonicalidia immobilizeduroporphyrinogenisynthetasefromrhodopseudomonaspalustris AT juknatadelaana immobilizeduroporphyrinogenisynthetasefromrhodopseudomonaspalustris AT batllealciramariadelcarmen immobilizeduroporphyrinogenisynthetasefromrhodopseudomonaspalustris |
| _version_ |
1768541567430164480 |