Porphyrin biosynthesis in Euglena gracilis-V. Soluble and particulate PBG-ASE

1. 1. Porphobilinogenase (PBG-ase) from soluble and particulate fractions of Euglena gracilis was isolated and purified. 2. 2. A highly efficient method for the dissociation of the membrane-bound enzyme using the chaotropic agent SCN is described. 3. 3. The chromatographic behaviour of both soluble...

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Autores principales: Rossetti, María Victoria, Lombardo, María Elisa, Juknat, Adela Ana, Araujo, Lidia Susana, Batlle, Alcira María del Carmen
Publicado: 1986
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v85_n2_p451_Rossetti
http://hdl.handle.net/20.500.12110/paper_03050491_v85_n2_p451_Rossetti
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spelling paper:paper_03050491_v85_n2_p451_Rossetti2023-06-08T15:30:22Z Porphyrin biosynthesis in Euglena gracilis-V. Soluble and particulate PBG-ASE Rossetti, María Victoria Lombardo, María Elisa Juknat, Adela Ana Araujo, Lidia Susana Batlle, Alcira María del Carmen 1. 1. Porphobilinogenase (PBG-ase) from soluble and particulate fractions of Euglena gracilis was isolated and purified. 2. 2. A highly efficient method for the dissociation of the membrane-bound enzyme using the chaotropic agent SCN is described. 3. 3. The chromatographic behaviour of both soluble and particulate PBG-ase on Sephadex G-100 and Sepharose 4B was quite similar but not identical. 4. 4. Euglena gracilis PBG-ase appears to exist in an equilibrium mixture of two active species of mol. wt 50,000 and 25,000. © 1986. Fil:Rossetti, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Lombardo, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Juknat De Geralnik, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Araujo, L.S. 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. 1986 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v85_n2_p451_Rossetti http://hdl.handle.net/20.500.12110/paper_03050491_v85_n2_p451_Rossetti
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
description 1. 1. Porphobilinogenase (PBG-ase) from soluble and particulate fractions of Euglena gracilis was isolated and purified. 2. 2. A highly efficient method for the dissociation of the membrane-bound enzyme using the chaotropic agent SCN is described. 3. 3. The chromatographic behaviour of both soluble and particulate PBG-ase on Sephadex G-100 and Sepharose 4B was quite similar but not identical. 4. 4. Euglena gracilis PBG-ase appears to exist in an equilibrium mixture of two active species of mol. wt 50,000 and 25,000. © 1986.
author Rossetti, María Victoria
Lombardo, María Elisa
Juknat, Adela Ana
Araujo, Lidia Susana
Batlle, Alcira María del Carmen
spellingShingle Rossetti, María Victoria
Lombardo, María Elisa
Juknat, Adela Ana
Araujo, Lidia Susana
Batlle, Alcira María del Carmen
Porphyrin biosynthesis in Euglena gracilis-V. Soluble and particulate PBG-ASE
author_facet Rossetti, María Victoria
Lombardo, María Elisa
Juknat, Adela Ana
Araujo, Lidia Susana
Batlle, Alcira María del Carmen
author_sort Rossetti, María Victoria
title Porphyrin biosynthesis in Euglena gracilis-V. Soluble and particulate PBG-ASE
title_short Porphyrin biosynthesis in Euglena gracilis-V. Soluble and particulate PBG-ASE
title_full Porphyrin biosynthesis in Euglena gracilis-V. Soluble and particulate PBG-ASE
title_fullStr Porphyrin biosynthesis in Euglena gracilis-V. Soluble and particulate PBG-ASE
title_full_unstemmed Porphyrin biosynthesis in Euglena gracilis-V. Soluble and particulate PBG-ASE
title_sort porphyrin biosynthesis in euglena gracilis-v. soluble and particulate pbg-ase
publishDate 1986
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v85_n2_p451_Rossetti
http://hdl.handle.net/20.500.12110/paper_03050491_v85_n2_p451_Rossetti
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