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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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
id todo:paper_NIS18665_v26_n5_p371_Rossetti
record_format dspace
spelling todo:paper_NIS18665_v26_n5_p371_Rossetti2023-10-03T16:46:10Z Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase Rossetti, M.V. Parera, V.E. Del Batlle, C.A.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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
Rossetti, M.V.
Parera, V.E.
Del Batlle, C.A.M.
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.
format JOUR
author Rossetti, M.V.
Parera, V.E.
Del Batlle, C.A.M.
author_facet Rossetti, M.V.
Parera, V.E.
Del Batlle, C.A.M.
author_sort Rossetti, M.V.
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
url http://hdl.handle.net/20.500.12110/paper_NIS18665_v26_n5_p371_Rossetti
work_keys_str_mv AT rossettimv porphyrinbiosynthesisimmobilizedenzymesandligandsviistudiesonbovineliverporphobilinogenase
AT parerave porphyrinbiosynthesisimmobilizedenzymesandligandsviistudiesonbovineliverporphobilinogenase
AT delbatllecam porphyrinbiosynthesisimmobilizedenzymesandligandsviistudiesonbovineliverporphobilinogenase
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