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  • Title: Ornithine decarboxylase in Trypanosoma brucei brucei: evidence for selective toxicity of difluoromethylornithine.
    Author: Garofalo J, Bacchi CJ, McLaughlin SD, Mockenhaupt D, Trueba G, Hutner SH.
    Journal: J Protozool; 1982 Aug; 29(3):389-94. PubMed ID: 6813460.
    Abstract:
    Activity of ornithine decarboxylase, the major rate limiting enzyme of polyamine biosynthesis, was determined in bloodstream trypomastigotes of Trypanosoma brucei brucei. The enzyme required pyridoxal-5'-phosphate, dithiothreitol and EDTA for optimal activity. Several properties of the enzyme were investigated and compared to the mammalian enzyme. Most notably, the parasite enzyme was greater than 60-fold more sensitive to the inhibitor DL-alpha-difluoromethylornithine than its mammalian counterpart, thus making it an attractive target for chemotherapy.
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