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
Publicado:	1976
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:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18665_v26_n5_p371_Rossetti 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

id	paper:paper_NIS18665_v26_n5_p371_Rossetti
record_format	dspace
spelling	paper:paper_NIS18665_v26_n5_p371_Rossetti2023-06-08T16:39:52Z Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase 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 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. 1976 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18665_v26_n5_p371_Rossetti http://hdl.handle.net/20.500.12110/paper_NIS18665_v26_n5_p371_Rossetti
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	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
spellingShingle	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 Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase
topic_facet	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
description	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.
title	Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase
title_short	Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase
title_full	Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase
title_fullStr	Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase
title_full_unstemmed	Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase
title_sort	porphyrin biosynthesis. immobilized enzymes and ligands. vii. studies on bovine liver porphobilinogenase
publishDate	1976
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18665_v26_n5_p371_Rossetti http://hdl.handle.net/20.500.12110/paper_NIS18665_v26_n5_p371_Rossetti
_version_	1769175828771373056

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

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