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
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00145793_v301_n3_p261_Ceriani
Acceder
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oai_identifier_str paperaa:paper_00145793_v301_n3_p261_Ceriani
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling 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/ar2025-10-23T11:18:28Zpaperaa: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:18962025-10-23 11:18:29.456Biblioteca 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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score 12.982451

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