Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose

Bovine liver aminolaevulate dehydratase (ALAD) has been chemically attached to Sepharose 4B and its properties have been studied. The optimal conditions for coupling have been determined. It was found that the immobilized enzyme retained a significant percentage of the activity of the free enzyme. T...

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Detalles Bibliográficos
Publicado:	1977
Materias:	enzyme liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p97_Stella http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p97_Stella
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_03008177_v16_n2-3_p97_Stella
record_format	dspace
spelling	paper:paper_03008177_v16_n2-3_p97_Stella2023-06-08T15:27:24Z Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose enzyme liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature Bovine liver aminolaevulate dehydratase (ALAD) has been chemically attached to Sepharose 4B and its properties have been studied. The optimal conditions for coupling have been determined. It was found that the immobilized enzyme retained a significant percentage of the activity of the free enzyme. The coupling yield was rather high. The insolubilized enzyme requires both anaerobiosis and a thiol activator for maximal activity. It can be stored at 4 °C for long periods with little loss of activity and it can be repeatedly used without alteration of its enzymic capacity. Attachment of ALA-D to the gel has led to an enhanced thermal stability. pH optima of free and bound enzyme was the same while a small decrease in the Km of the matrix bonded ALA-D as compared to that of the soluble enzyme was observed. The use of the fixed-ALA-D for the preparation of PBG is described. © 1977 Dr. W. Junk b.v. Publishers. 1977 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p97_Stella http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p97_Stella
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 liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature
spellingShingle	enzyme liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose
topic_facet	enzyme liver enzyme porphobilinogen synthase porphyrin cattle in vitro study theoretical study Animal Cattle Comparative Study Drug Stability Enzymes, Immobilized Hydro-Lyases Hydrogen-Ion Concentration Kinetics Liver Methods Porphobilinogen Porphobilinogen Synthase Sepharose Temperature
description	Bovine liver aminolaevulate dehydratase (ALAD) has been chemically attached to Sepharose 4B and its properties have been studied. The optimal conditions for coupling have been determined. It was found that the immobilized enzyme retained a significant percentage of the activity of the free enzyme. The coupling yield was rather high. The insolubilized enzyme requires both anaerobiosis and a thiol activator for maximal activity. It can be stored at 4 °C for long periods with little loss of activity and it can be repeatedly used without alteration of its enzymic capacity. Attachment of ALA-D to the gel has led to an enhanced thermal stability. pH optima of free and bound enzyme was the same while a small decrease in the Km of the matrix bonded ALA-D as compared to that of the soluble enzyme was observed. The use of the fixed-ALA-D for the preparation of PBG is described. © 1977 Dr. W. Junk b.v. Publishers.
title	Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose
title_short	Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose
title_full	Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose
title_fullStr	Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose
title_full_unstemmed	Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose
title_sort	porphyrin biosynthesis. immobilized enzymes iv. studies on aminolaevulate dehydratase attached to sepharose
publishDate	1977
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p97_Stella http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p97_Stella
_version_	1768543559240122368

Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose

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