Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase

Bovine liver porphobilinogenase (PBGase) has been covalently attached to Sepharose, and some of their properties have been studied. The optimal conditions for binding have been determined. The water-insoluble PBGase retained a high percentage of the activity of the soluble enzyme; the coupling yield...

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Detalles Bibliográficos
Autores principales: Rossetti, M.V., Parera, V.E., Del Batlle, C.A.M.
Formato: JOUR
Materias:
enzyme
porphyrin
animal experiment
cattle
in vitro study
liver
porphobilinogenase
Ammonia-Lyases
Animal
Cattle
Enzymes, Immobilized
Hydrogen-Ion Concentration
Ligands
Liver
Porphyrins
Protein Binding
Sepharose
Temperature
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_NIS18665_v26_n5_p371_Rossetti
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:Bovine liver porphobilinogenase (PBGase) has been covalently attached to Sepharose, and some of their properties have been studied. The optimal conditions for binding have been determined. The water-insoluble PBGase retained a high percentage of the activity of the soluble enzyme; the coupling yield was also high. Sepharose-PBGase could be stored at 4°C for periods up to 5 weeks with 40% loss of activity and it could be repeatedly used with little alteration of its enzymic activity; however, both by storage and repeated use, isomerase was inactivated and the percentage of uroporphyrinogen I formed was increased. Attachment of PBGase to Sepharose has led to enhanced thermal stability. pH optima of the insolubilized enzyme was shifted 0.6 units towards the alkaline side as compared to that of the native enzyme.

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