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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_0020711X_v12_n5-6_p729_Viale
Ver los metadatos del registro completo
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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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1844618735047933952 |
score |
13.070432 |