Porphyrin biosynthesis-immobilized enzymes and ligands VIII. Studies on the purification of δ-aminolaevulinate dehydratase from Euglena gracilis

Highly stable selective adsorbents for δ-aminolaevulinate dehydratase (ALA-D) were prepared by attaching the substrate to agarose beads, either directly or through an extension arm. Columns containing these biospecific adsorbents can completely bind the enzyme present in extracts of Euglena gracilis...

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Autores principales: Stella, A.M., del C. Batlle, A.M.
Formato: JOUR
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03044211_v11_n2_p87_Stella
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_03044211_v11_n2_p87_Stella2023-10-03T15:20:52Z Porphyrin biosynthesis-immobilized enzymes and ligands VIII. Studies on the purification of δ-aminolaevulinate dehydratase from Euglena gracilis Stella, A.M. del C. Batlle, A.M. Highly stable selective adsorbents for δ-aminolaevulinate dehydratase (ALA-D) were prepared by attaching the substrate to agarose beads, either directly or through an extension arm. Columns containing these biospecific adsorbents can completely bind the enzyme present in extracts of Euglena gracilis Z strain. Elution is obtained by changing the ionic strength of the buffer. Due to their ease of preparation and high stability these adsorbents may be of general value for purification of ALA-D from different sources. © 1978. Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03044211_v11_n2_p87_Stella
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
description Highly stable selective adsorbents for δ-aminolaevulinate dehydratase (ALA-D) were prepared by attaching the substrate to agarose beads, either directly or through an extension arm. Columns containing these biospecific adsorbents can completely bind the enzyme present in extracts of Euglena gracilis Z strain. Elution is obtained by changing the ionic strength of the buffer. Due to their ease of preparation and high stability these adsorbents may be of general value for purification of ALA-D from different sources. © 1978.
format JOUR
author Stella, A.M.
del C. Batlle, A.M.
spellingShingle Stella, A.M.
del C. Batlle, A.M.
Porphyrin biosynthesis-immobilized enzymes and ligands VIII. Studies on the purification of δ-aminolaevulinate dehydratase from Euglena gracilis
author_facet Stella, A.M.
del C. Batlle, A.M.
author_sort Stella, A.M.
title Porphyrin biosynthesis-immobilized enzymes and ligands VIII. Studies on the purification of δ-aminolaevulinate dehydratase from Euglena gracilis
title_short Porphyrin biosynthesis-immobilized enzymes and ligands VIII. Studies on the purification of δ-aminolaevulinate dehydratase from Euglena gracilis
title_full Porphyrin biosynthesis-immobilized enzymes and ligands VIII. Studies on the purification of δ-aminolaevulinate dehydratase from Euglena gracilis
title_fullStr Porphyrin biosynthesis-immobilized enzymes and ligands VIII. Studies on the purification of δ-aminolaevulinate dehydratase from Euglena gracilis
title_full_unstemmed Porphyrin biosynthesis-immobilized enzymes and ligands VIII. Studies on the purification of δ-aminolaevulinate dehydratase from Euglena gracilis
title_sort porphyrin biosynthesis-immobilized enzymes and ligands viii. studies on the purification of δ-aminolaevulinate dehydratase from euglena gracilis
url http://hdl.handle.net/20.500.12110/paper_03044211_v11_n2_p87_Stella
work_keys_str_mv AT stellaam porphyrinbiosynthesisimmobilizedenzymesandligandsviiistudiesonthepurificationofdaminolaevulinatedehydratasefromeuglenagracilis
AT delcbatlleam porphyrinbiosynthesisimmobilizedenzymesandligandsviiistudiesonthepurificationofdaminolaevulinatedehydratasefromeuglenagracilis
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