Abstract
The pyruvate dehydrogense complex (PDC) has been purified to apparent homogeneity from 2 parasitic helminths exhibiting anaerobic mitochondrial metabolism, the equine nematode,
Parascaris equorum, and the canine cestode,
Dipylidium caninum. The
P. equorum PDC yielded 7 major bands when separated by SDS-PAGE. The bands of 72, 55-53.5, 41 and 36 kDa corresponded to E2, E3, E1α and E1β, respectively. The complex also contained additional unidentified proteins of 43 and 45 kDa. Incubation of the complex with [2-
14C]pyruvate resulted in the acetylation of only E2. These results suggest that the
P. equorum PDC lacks protein X and exhibits an altered subunit composition, as has been described previously for the PDC of the related nematode,
Ascaris suum. In contrast, the
D. caninum PDC yielded only four major bands after SDS-PAGE of 59, 58, 39 and 34 kDa, which corresponded to E3, E2, E1α and E1β, respectively. Incubation of the
D. caninum complex with [2-
14C]pyruvate resulted in the acetylation of E2 and a second protein which comigrated with E3, suggesting that the
D. caninum complex contained protein X and had a subunit composition similar to PDCs from other eukaryotic organisms. Both helminth complexes appeared less sensitive to inhibition by elevated NADH/NAD
+ ratios than complexes isolated from aerobic organisms, as would be predicted for PDCs from organisms exploiting microaerobic habitats. These results suggest that although these helminths have similar anerobic mitochondrial pathways, they contain significantly different PDCs.
