Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation

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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 mi...

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Detalles Bibliográficos
Autores principales: Ceriani, C., González, N.S., Algranati, I.D.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 1992
Materias:
Crithidia fasciculata
Enzyme turnover
Ornithine decarboxylase
Polyamine-dependent regulation
ornithine decarboxylase
polyamine
article
crithidia fasciculata
down regulation
nonhuman
priority journal
protein metabolism
Animal
Catalysis
Down-Regulation
Ornithine Decarboxylase
Polyamines
Putrescine
Support, Non-U.S. Gov't
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00145793_v301_n3_p261_Ceriani
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling paperaa:paper_00145793_v301_n3_p261_Ceriani2023-06-12T16:41:48Z Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation FEBS Lett. 1992;301(3):261-264 Ceriani, C. González, N.S. Algranati, I.D. 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 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. 1992 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00145793_v301_n3_p261_Ceriani
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language Inglés
orig_language_str_mv eng
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
spellingShingle 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
Ceriani, C.
González, N.S.
Algranati, I.D.
Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation
topic_facet 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
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.
format Artículo
Artículo
publishedVersion
author Ceriani, C.
González, N.S.
Algranati, I.D.
author_facet Ceriani, C.
González, N.S.
Algranati, I.D.
author_sort Ceriani, C.
title Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation
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
publishDate 1992
url http://hdl.handle.net/20.500.12110/paper_00145793_v301_n3_p261_Ceriani
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AT gonzalezns ornithinedecarboxylasefromcrithidiafasciculataismetabolicallyunstableandresistanttopolyaminedownregulation
AT algranatiid ornithinedecarboxylasefromcrithidiafasciculataismetabolicallyunstableandresistanttopolyaminedownregulation
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