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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Detalles Bibliográficos
Autores principales: Kotler, M.L., Juknat, A.A., Batlle, A.M.D.C.
Formato: JOUR
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_08854513_v12_n3_p252_Kotler
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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

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