Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation
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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1992
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Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00145793_v301_n3_p261_Ceriani |
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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 |
work_keys_str_mv |
AT cerianic ornithinedecarboxylasefromcrithidiafasciculataismetabolicallyunstableandresistanttopolyaminedownregulation AT gonzalezns ornithinedecarboxylasefromcrithidiafasciculataismetabolicallyunstableandresistanttopolyaminedownregulation AT algranatiid ornithinedecarboxylasefromcrithidiafasciculataismetabolicallyunstableandresistanttopolyaminedownregulation |
_version_ |
1769810263594237952 |