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
| Documento: | Artículo |
| Título: | Immobilized uroporphyrinogen I synthetase from Rhodopseudomonas palustris |
| Autor: | Kotler, M.L.; Juknat, A.A.; Batlle, A.M.D.C. |
| Filiación: | Centro de Investigaciones sobre Porfirinas y Porfirias, Ciudad Universitaria, Buenos Aires, Argentina |
| Palabras clave: | 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 |
| Año: | 1990 |
| Volumen: | 12 |
| Número: | 3 |
| Página de inicio: | 252 |
| Página de fin: | 257 |
| DOI: | http://dx.doi.org/10.1111/j.1470-8744.1990.tb00097.x |
| Título revista: | Biotechnology and Applied Biochemistry |
| Título revista abreviado: | Biotechnol. Appl. Biochem. |
| ISSN: | 08854513 |
| CAS: | Ammonia-Lyases, EC 4.3.1.; Enzymes, Immobilized; Hydroxymethylbilane Synthase, EC 4.3.1.8; Sepharose, 9012-36-6 |
| Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08854513_v12_n3_p252_Kotler |
