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Arginine kinase of the flagellate protozoa Trypanosoma cruzi
Author(s) -
Alonso Guillermo D,
Pereira Claudio A,
Remedi Marı́a S,
Paveto M.Cristina,
Cochella Luisa,
Ivaldi M.Soledad,
Gerez de Burgos Nelia M,
Torres Héctor N,
Flawiá Mirtha M
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02473-5
Subject(s) - trypanosoma cruzi , arginine kinase , arginine , biochemistry , biology , enzyme , kinase , enzyme assay , protozoa , microbiology and biotechnology , amino acid , parasite hosting , computer science , world wide web
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.