Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity

Autores
Viale, A.A.; De Xifra, E.A.W.; Del C. Batlle, A.M.
Año de publicación
1980
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
1. 1. No changes in ALA-S activity were observed when different preparations of R. palustris were stored at 4°C for various periods of time. 2. 2. Mixing supernatants from pigmented and decoloured R. palustris cells, showed that the activity of ALA-S was several times higher than expected, suggesting the presence of an activator. 3. 3. Supernatants from photosynthetically and aerobically grown cells were heated and the effect of the protein-free supernatant was tested on both red and white supernatants. The heated supernatant from aerobic cells increased ALA-S when added to red and white preparations, but the heated red supernatant only activated red supernatant and had no action on the white cells enzyme. 4. 4. By gel filtration on Sephadex G-25 of cell free extracts from R. palustris either aerobically or anaerobically grown, a low molecular weight compound was separated, which added back to the homologeous enzyme enhanced its activity confirming the existence of one or two low-molecular weight and heat-stable factors which would act stimulating ALA-S activity. 5. 5. A scheme is proposed to explain the role of these factors on the control of ALA-S in R. palustris. © 1980.
Fil:Viale, A.A. 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.
Fuente
Int. J. Biochem. 1980;12(5-6):729-733
Materia
5 aminolevulinate synthase
porphyrin
aerobic metabolism
article
biosynthesis
kinetics
metabolism
molecular weight
photosynthesis
Rhodopseudomonas
5-Aminolevulinate Synthetase
Aerobiosis
Kinetics
Molecular Weight
Photosynthesis
Porphyrins
Rhodopseudomonas
Support, Non-U.S. Gov't
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_0020711X_v12_n5-6_p729_Viale

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oai_identifier_str paperaa:paper_0020711X_v12_n5-6_p729_Viale
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activityViale, A.A.De Xifra, E.A.W.Del C. Batlle, A.M.5 aminolevulinate synthaseporphyrinaerobic metabolismarticlebiosynthesiskineticsmetabolismmolecular weightphotosynthesisRhodopseudomonas5-Aminolevulinate SynthetaseAerobiosisKineticsMolecular WeightPhotosynthesisPorphyrinsRhodopseudomonasSupport, Non-U.S. Gov't1. 1. No changes in ALA-S activity were observed when different preparations of R. palustris were stored at 4°C for various periods of time. 2. 2. Mixing supernatants from pigmented and decoloured R. palustris cells, showed that the activity of ALA-S was several times higher than expected, suggesting the presence of an activator. 3. 3. Supernatants from photosynthetically and aerobically grown cells were heated and the effect of the protein-free supernatant was tested on both red and white supernatants. The heated supernatant from aerobic cells increased ALA-S when added to red and white preparations, but the heated red supernatant only activated red supernatant and had no action on the white cells enzyme. 4. 4. By gel filtration on Sephadex G-25 of cell free extracts from R. palustris either aerobically or anaerobically grown, a low molecular weight compound was separated, which added back to the homologeous enzyme enhanced its activity confirming the existence of one or two low-molecular weight and heat-stable factors which would act stimulating ALA-S activity. 5. 5. A scheme is proposed to explain the role of these factors on the control of ALA-S in R. palustris. © 1980.Fil:Viale, A.A. 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.1980info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p729_VialeInt. J. Biochem. 1980;12(5-6):729-733reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:42:54Zpaperaa:paper_0020711X_v12_n5-6_p729_VialeInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:42:56.081Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity
title Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity
spellingShingle Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity
Viale, A.A.
5 aminolevulinate synthase
porphyrin
aerobic metabolism
article
biosynthesis
kinetics
metabolism
molecular weight
photosynthesis
Rhodopseudomonas
5-Aminolevulinate Synthetase
Aerobiosis
Kinetics
Molecular Weight
Photosynthesis
Porphyrins
Rhodopseudomonas
Support, Non-U.S. Gov't
title_short Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity
title_full Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity
title_fullStr Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity
title_full_unstemmed Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity
title_sort Porphyrin biosynthesis in rhodopseudomonas palustris-II. Evidence on the existence of a factor regulating aminolevulinate synthetase activity
dc.creator.none.fl_str_mv Viale, A.A.
De Xifra, E.A.W.
Del C. Batlle, A.M.
author Viale, A.A.
author_facet Viale, A.A.
De Xifra, E.A.W.
Del C. Batlle, A.M.
author_role author
author2 De Xifra, E.A.W.
Del C. Batlle, A.M.
author2_role author
author
dc.subject.none.fl_str_mv 5 aminolevulinate synthase
porphyrin
aerobic metabolism
article
biosynthesis
kinetics
metabolism
molecular weight
photosynthesis
Rhodopseudomonas
5-Aminolevulinate Synthetase
Aerobiosis
Kinetics
Molecular Weight
Photosynthesis
Porphyrins
Rhodopseudomonas
Support, Non-U.S. Gov't
topic 5 aminolevulinate synthase
porphyrin
aerobic metabolism
article
biosynthesis
kinetics
metabolism
molecular weight
photosynthesis
Rhodopseudomonas
5-Aminolevulinate Synthetase
Aerobiosis
Kinetics
Molecular Weight
Photosynthesis
Porphyrins
Rhodopseudomonas
Support, Non-U.S. Gov't
dc.description.none.fl_txt_mv 1. 1. No changes in ALA-S activity were observed when different preparations of R. palustris were stored at 4°C for various periods of time. 2. 2. Mixing supernatants from pigmented and decoloured R. palustris cells, showed that the activity of ALA-S was several times higher than expected, suggesting the presence of an activator. 3. 3. Supernatants from photosynthetically and aerobically grown cells were heated and the effect of the protein-free supernatant was tested on both red and white supernatants. The heated supernatant from aerobic cells increased ALA-S when added to red and white preparations, but the heated red supernatant only activated red supernatant and had no action on the white cells enzyme. 4. 4. By gel filtration on Sephadex G-25 of cell free extracts from R. palustris either aerobically or anaerobically grown, a low molecular weight compound was separated, which added back to the homologeous enzyme enhanced its activity confirming the existence of one or two low-molecular weight and heat-stable factors which would act stimulating ALA-S activity. 5. 5. A scheme is proposed to explain the role of these factors on the control of ALA-S in R. palustris. © 1980.
Fil:Viale, A.A. 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.
description 1. 1. No changes in ALA-S activity were observed when different preparations of R. palustris were stored at 4°C for various periods of time. 2. 2. Mixing supernatants from pigmented and decoloured R. palustris cells, showed that the activity of ALA-S was several times higher than expected, suggesting the presence of an activator. 3. 3. Supernatants from photosynthetically and aerobically grown cells were heated and the effect of the protein-free supernatant was tested on both red and white supernatants. The heated supernatant from aerobic cells increased ALA-S when added to red and white preparations, but the heated red supernatant only activated red supernatant and had no action on the white cells enzyme. 4. 4. By gel filtration on Sephadex G-25 of cell free extracts from R. palustris either aerobically or anaerobically grown, a low molecular weight compound was separated, which added back to the homologeous enzyme enhanced its activity confirming the existence of one or two low-molecular weight and heat-stable factors which would act stimulating ALA-S activity. 5. 5. A scheme is proposed to explain the role of these factors on the control of ALA-S in R. palustris. © 1980.
publishDate 1980
dc.date.none.fl_str_mv 1980
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p729_Viale
url http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p729_Viale
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Int. J. Biochem. 1980;12(5-6):729-733
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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