Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation
- Autores
- Ceriani, C.; González, N.S.; Algranati, I.D.
- Año de publicación
- 1992
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Ornithine decarboxylase (ODC) of Crithidia fasciculata extracts shows maximal activity during exponential growth of the parasite and decreases markedly in the stationary phase. The inhibition of protein synthesis by cycloheximide evoked a rapid loss of enzyme activity with a half-life of about 30 min. Upon removal of DFMO from Crithidia cultures treated with the drug for 24 h, the ODC activity increased at the same rate as total protein synthesis. The addition of putrescine at high concentrations to parasites cultivated in a synthetic medium showed that Crithidia CDC levels were not reduced by polyamines. © 1992.
Fil:Ceriani, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. - Fuente
- FEBS Lett. 1992;301(3):261-264
- Materia
-
Crithidia fasciculata
Enzyme turnover
Ornithine decarboxylase
Polyamine-dependent regulation
ornithine decarboxylase
polyamine
article
crithidia fasciculata
down regulation
nonhuman
priority journal
protein metabolism
Animal
Catalysis
Crithidia fasciculata
Down-Regulation
Ornithine Decarboxylase
Polyamines
Putrescine
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_00145793_v301_n3_p261_Ceriani
Ver los metadatos del registro completo
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Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulationCeriani, C.González, N.S.Algranati, I.D.Crithidia fasciculataEnzyme turnoverOrnithine decarboxylasePolyamine-dependent regulationornithine decarboxylasepolyaminearticlecrithidia fasciculatadown regulationnonhumanpriority journalprotein metabolismAnimalCatalysisCrithidia fasciculataDown-RegulationOrnithine DecarboxylasePolyaminesPutrescineSupport, Non-U.S. Gov'tOrnithine decarboxylase (ODC) of Crithidia fasciculata extracts shows maximal activity during exponential growth of the parasite and decreases markedly in the stationary phase. The inhibition of protein synthesis by cycloheximide evoked a rapid loss of enzyme activity with a half-life of about 30 min. Upon removal of DFMO from Crithidia cultures treated with the drug for 24 h, the ODC activity increased at the same rate as total protein synthesis. The addition of putrescine at high concentrations to parasites cultivated in a synthetic medium showed that Crithidia CDC levels were not reduced by polyamines. © 1992.Fil:Ceriani, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1992info: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_00145793_v301_n3_p261_CerianiFEBS Lett. 1992;301(3):261-264reponame: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/ar2025-09-29T13:43:03Zpaperaa:paper_00145793_v301_n3_p261_CerianiInstitucionalhttps://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 13:43:04.374Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse |
dc.title.none.fl_str_mv |
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation |
title |
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation |
spellingShingle |
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation Ceriani, C. Crithidia fasciculata Enzyme turnover Ornithine decarboxylase Polyamine-dependent regulation ornithine decarboxylase polyamine article crithidia fasciculata down regulation nonhuman priority journal protein metabolism Animal Catalysis Crithidia fasciculata Down-Regulation Ornithine Decarboxylase Polyamines Putrescine Support, Non-U.S. Gov't |
title_short |
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation |
title_full |
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation |
title_fullStr |
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation |
title_full_unstemmed |
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation |
title_sort |
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation |
dc.creator.none.fl_str_mv |
Ceriani, C. González, N.S. Algranati, I.D. |
author |
Ceriani, C. |
author_facet |
Ceriani, C. González, N.S. Algranati, I.D. |
author_role |
author |
author2 |
González, N.S. Algranati, I.D. |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Crithidia fasciculata Enzyme turnover Ornithine decarboxylase Polyamine-dependent regulation ornithine decarboxylase polyamine article crithidia fasciculata down regulation nonhuman priority journal protein metabolism Animal Catalysis Crithidia fasciculata Down-Regulation Ornithine Decarboxylase Polyamines Putrescine Support, Non-U.S. Gov't |
topic |
Crithidia fasciculata Enzyme turnover Ornithine decarboxylase Polyamine-dependent regulation ornithine decarboxylase polyamine article crithidia fasciculata down regulation nonhuman priority journal protein metabolism Animal Catalysis Crithidia fasciculata Down-Regulation Ornithine Decarboxylase Polyamines Putrescine Support, Non-U.S. Gov't |
dc.description.none.fl_txt_mv |
Ornithine decarboxylase (ODC) of Crithidia fasciculata extracts shows maximal activity during exponential growth of the parasite and decreases markedly in the stationary phase. The inhibition of protein synthesis by cycloheximide evoked a rapid loss of enzyme activity with a half-life of about 30 min. Upon removal of DFMO from Crithidia cultures treated with the drug for 24 h, the ODC activity increased at the same rate as total protein synthesis. The addition of putrescine at high concentrations to parasites cultivated in a synthetic medium showed that Crithidia CDC levels were not reduced by polyamines. © 1992. Fil:Ceriani, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. |
description |
Ornithine decarboxylase (ODC) of Crithidia fasciculata extracts shows maximal activity during exponential growth of the parasite and decreases markedly in the stationary phase. The inhibition of protein synthesis by cycloheximide evoked a rapid loss of enzyme activity with a half-life of about 30 min. Upon removal of DFMO from Crithidia cultures treated with the drug for 24 h, the ODC activity increased at the same rate as total protein synthesis. The addition of putrescine at high concentrations to parasites cultivated in a synthetic medium showed that Crithidia CDC levels were not reduced by polyamines. © 1992. |
publishDate |
1992 |
dc.date.none.fl_str_mv |
1992 |
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_00145793_v301_n3_p261_Ceriani |
url |
http://hdl.handle.net/20.500.12110/paper_00145793_v301_n3_p261_Ceriani |
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 |
FEBS Lett. 1992;301(3):261-264 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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1844618738148573184 |
score |
13.070432 |