Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography

1. 1. Fully reversible and highly stable biospecific adsorbents have been prepared by attaching delta aminolaevulinate to cyanogen bromide activated-Sepharose 4B, either directly or through extension arms. 2. 2. Purification of bovine liver delta aminolaevulinate dehydratase by means of these select...

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Autores principales: Stella, A.M., del C. Batlle, A.M.
Formato: JOUR
Materias:
liver enzyme
porphobilinogen synthase
porphyrin
cattle
in vitro study
methodology
theoretical study
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v8_n5_p353_Stella
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_0020711X_v8_n5_p353_Stella
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spelling todo:paper_0020711X_v8_n5_p353_Stella2023-10-03T14:18:13Z Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography Stella, A.M. del C. Batlle, A.M. liver enzyme porphobilinogen synthase porphyrin cattle in vitro study methodology theoretical study 1. 1. Fully reversible and highly stable biospecific adsorbents have been prepared by attaching delta aminolaevulinate to cyanogen bromide activated-Sepharose 4B, either directly or through extension arms. 2. 2. Purification of bovine liver delta aminolaevulinate dehydratase by means of these selective adsorbents is reported. These materials adsorb the enzyme quantitatively from partially purified preparations, and elution of delta aminolaevulinate dehydratase is achieved by modifying the ionic strength of the buffer. © 1977. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v8_n5_p353_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 liver enzyme
porphobilinogen synthase
porphyrin
cattle
in vitro study
methodology
theoretical study
spellingShingle liver enzyme
porphobilinogen synthase
porphyrin
cattle
in vitro study
methodology
theoretical study
Stella, A.M.
del C. Batlle, A.M.
Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
topic_facet liver enzyme
porphobilinogen synthase
porphyrin
cattle
in vitro study
methodology
theoretical study
description 1. 1. Fully reversible and highly stable biospecific adsorbents have been prepared by attaching delta aminolaevulinate to cyanogen bromide activated-Sepharose 4B, either directly or through extension arms. 2. 2. Purification of bovine liver delta aminolaevulinate dehydratase by means of these selective adsorbents is reported. These materials adsorb the enzyme quantitatively from partially purified preparations, and elution of delta aminolaevulinate dehydratase is achieved by modifying the ionic strength of the buffer. © 1977.
format JOUR
author Stella, A.M.
del C. Batlle, A.M.
author_facet Stella, A.M.
del C. Batlle, A.M.
author_sort Stella, A.M.
title Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
title_short Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
title_full Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
title_fullStr Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
title_full_unstemmed Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
title_sort porphyrin biosynthesis-immobilized enzymes and ligands-v. purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
url http://hdl.handle.net/20.500.12110/paper_0020711X_v8_n5_p353_Stella
work_keys_str_mv AT stellaam porphyrinbiosynthesisimmobilizedenzymesandligandsvpurificationofaminolaevulinatedehydratasefrombovineliverbyaffinitychromatography
AT delcbatlleam porphyrinbiosynthesisimmobilizedenzymesandligandsvpurificationofaminolaevulinatedehydratasefrombovineliverbyaffinitychromatography
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