Abstract
A trypanothione-dependent peroxidase activity has been identified in the insect trypanosomatid Crithidia fasciculata and in the mammalian trypanosome Trypanosoma brucei. Using organic hydroperoxides as oxidant, specific peroxidase activities in these organisms are 5.0 and 1.0 nmol min-1 (108 cells)-1 respectively. The T. brucei peroxidase had an activity of 0.4 nmol min-1 (108 cells)-1 using hydrogen peroxide as oxidant. The enzyme is specific for the N1,N8-bis(glutathionyl)spermidine conjugate (dihydrotrypanothione); N1-mono-glutathionylspermidine is not a substrate. Experiments to demonstrate that this parasite peroxidase may contain selenium were inconclusive. However, bloodstream T. brucei can incorporate radiolabelled selenite into proteins.
Original language | English |
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Pages (from-to) | 39-45 |
Number of pages | 7 |
Journal | Molecular and Biochemical Parasitology |
Volume | 24 |
Issue number | 1 |
DOIs | |
Publication status | Published - May 1987 |
Keywords
- Crithidia fasciculata
- Peroxide metabolism
- Trypanosoma brucei
- Trypanothione
ASJC Scopus subject areas
- Parasitology
- Molecular Biology