The phospholipases of Trypanosoma brucei bloodstream forms and cultured procyclics.
(1982) Molecular and Biochemical Parasitology — Vol. 5, n° 5, p. 309-319 (1982)
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- Phospholipase from Trypanosoma brucei bloodstream forms was characterized and subsequently localized. The enzyme had a specific activity of 100 nmol . min-1 . mg-1 protein. The major portion (greater than 90%) was a soluble phospholipase A1 with a pH optimum around 6; the remainder, also phospholipase A1, was particle-bound and had an optimal activity around pH 5.2. Both enzymes were maximally activated by 0.2% Triton X-100 but differed in their sensitivity towards the inhibitory action of higher concentrations of this detergent and diisopropyl fluorophosphate, the particle-bound activity being more sensitive than the soluble one. Cell fractionation showed that the particle-bound, more acidic phospholipase A1 was associated with alpha-mannosidase- and acid proteinase-containing lysosomes. Cultured procyclic trypomastigotes also contained phospholipase A but its specific activity was only 15% of that of bloodstream forms. This drastic reduction in overall activity upon transformation from bloodstream to culture form was the result of a decrease in soluble phospholipase, whereas the lysosomal activity essentially remained unchanged.
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Opperdoes, F., & Van Roy, J. (1982). The phospholipases of Trypanosoma brucei bloodstream forms and cultured procyclics. Molecular and Biochemical Parasitology, 5(5), 309-319. https://doi.org/10.1016/0166-6851(82)90038-X (Original work published 1982)