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: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v301_n3_p261_Ceriani http://hdl.handle.net/20.500.12110/paper_00145793_v301_n3_p261_Ceriani |
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paper:paper_00145793_v301_n3_p261_Ceriani2023-06-08T14:37:36Z Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation Ceriani, María Carolina González, Nélida Susana Algranati, Israel David 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 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v301_n3_p261_Ceriani 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) |
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, María Carolina González, Nélida Susana Algranati, Israel David 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. |
author |
Ceriani, María Carolina González, Nélida Susana Algranati, Israel David |
author_facet |
Ceriani, María Carolina González, Nélida Susana Algranati, Israel David |
author_sort |
Ceriani, María Carolina |
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 |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v301_n3_p261_Ceriani http://hdl.handle.net/20.500.12110/paper_00145793_v301_n3_p261_Ceriani |
work_keys_str_mv |
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_version_ |
1768542920169750528 |