Arginine kinase of the flagellate protozoa Trypanosoma cruzi: Regulation of its expression and catalytic activity
In epimastigotes of Trypanosoma cruzi, the etiological agent of Chagas' disease, arginine kinase activity increased continuously during the exponential phase of growth. A correlation between growth rate, enzyme-specific activity and enzyme protein was observed. Arginine kinase-specific activity...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00145793_v498_n1_p22_Alonso |
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todo:paper_00145793_v498_n1_p22_Alonso2023-10-03T14:13:06Z Arginine kinase of the flagellate protozoa Trypanosoma cruzi: Regulation of its expression and catalytic activity Alonso, G.D. Pereira, C.A. Remedi, M.S. Paveto, M.Cristina Cochella, L. Ivaldi, M.Soledad Gerez de Burgos, N.M. Torres, H.N. Flawiá, M.M. Arginine kinase Guanidino kinase Phosphagen Phosphoarginine Trypanosoma cruzi arginine kinase article energy expenditure enzyme activity enzyme specificity nonhuman priority journal protein expression starvation Trypanosoma cruzi Animals Arginine Kinase Cell Division Culture Media Gene Expression Regulation, Enzymologic Trypanosoma cruzi Mastigophora (flagellates) Protozoa Trypanosoma Trypanosoma cruzi In epimastigotes of Trypanosoma cruzi, the etiological agent of Chagas' disease, arginine kinase activity increased continuously during the exponential phase of growth. A correlation between growth rate, enzyme-specific activity and enzyme protein was observed. Arginine kinase-specific activity, expressed as a function of enzyme protein, remains roughly constant up to 18 days of culture. In the whole range of the culture time mRNA levels showed minor changes indicating that the enzyme activity is post-transcriptionally regulated. Arginine kinase could be proposed as a modulator of energetic reserves under starvation stress condition. © 2001 Federation of European Biochemical Societies. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00145793_v498_n1_p22_Alonso |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Arginine kinase Guanidino kinase Phosphagen Phosphoarginine Trypanosoma cruzi arginine kinase article energy expenditure enzyme activity enzyme specificity nonhuman priority journal protein expression starvation Trypanosoma cruzi Animals Arginine Kinase Cell Division Culture Media Gene Expression Regulation, Enzymologic Trypanosoma cruzi Mastigophora (flagellates) Protozoa Trypanosoma Trypanosoma cruzi |
| spellingShingle |
Arginine kinase Guanidino kinase Phosphagen Phosphoarginine Trypanosoma cruzi arginine kinase article energy expenditure enzyme activity enzyme specificity nonhuman priority journal protein expression starvation Trypanosoma cruzi Animals Arginine Kinase Cell Division Culture Media Gene Expression Regulation, Enzymologic Trypanosoma cruzi Mastigophora (flagellates) Protozoa Trypanosoma Trypanosoma cruzi Alonso, G.D. Pereira, C.A. Remedi, M.S. Paveto, M.Cristina Cochella, L. Ivaldi, M.Soledad Gerez de Burgos, N.M. Torres, H.N. Flawiá, M.M. Arginine kinase of the flagellate protozoa Trypanosoma cruzi: Regulation of its expression and catalytic activity |
| topic_facet |
Arginine kinase Guanidino kinase Phosphagen Phosphoarginine Trypanosoma cruzi arginine kinase article energy expenditure enzyme activity enzyme specificity nonhuman priority journal protein expression starvation Trypanosoma cruzi Animals Arginine Kinase Cell Division Culture Media Gene Expression Regulation, Enzymologic Trypanosoma cruzi Mastigophora (flagellates) Protozoa Trypanosoma Trypanosoma cruzi |
| description |
In epimastigotes of Trypanosoma cruzi, the etiological agent of Chagas' disease, arginine kinase activity increased continuously during the exponential phase of growth. A correlation between growth rate, enzyme-specific activity and enzyme protein was observed. Arginine kinase-specific activity, expressed as a function of enzyme protein, remains roughly constant up to 18 days of culture. In the whole range of the culture time mRNA levels showed minor changes indicating that the enzyme activity is post-transcriptionally regulated. Arginine kinase could be proposed as a modulator of energetic reserves under starvation stress condition. © 2001 Federation of European Biochemical Societies. |
| format |
JOUR |
| author |
Alonso, G.D. Pereira, C.A. Remedi, M.S. Paveto, M.Cristina Cochella, L. Ivaldi, M.Soledad Gerez de Burgos, N.M. Torres, H.N. Flawiá, M.M. |
| author_facet |
Alonso, G.D. Pereira, C.A. Remedi, M.S. Paveto, M.Cristina Cochella, L. Ivaldi, M.Soledad Gerez de Burgos, N.M. Torres, H.N. Flawiá, M.M. |
| author_sort |
Alonso, G.D. |
| title |
Arginine kinase of the flagellate protozoa Trypanosoma cruzi: Regulation of its expression and catalytic activity |
| title_short |
Arginine kinase of the flagellate protozoa Trypanosoma cruzi: Regulation of its expression and catalytic activity |
| title_full |
Arginine kinase of the flagellate protozoa Trypanosoma cruzi: Regulation of its expression and catalytic activity |
| title_fullStr |
Arginine kinase of the flagellate protozoa Trypanosoma cruzi: Regulation of its expression and catalytic activity |
| title_full_unstemmed |
Arginine kinase of the flagellate protozoa Trypanosoma cruzi: Regulation of its expression and catalytic activity |
| title_sort |
arginine kinase of the flagellate protozoa trypanosoma cruzi: regulation of its expression and catalytic activity |
| url |
http://hdl.handle.net/20.500.12110/paper_00145793_v498_n1_p22_Alonso |
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