Superoxide dismutase in cestodes. Isoenzymatic characterization and studies of inhibition by a series of benzimidazoles and by pyrimidine derivatives of recent synthesis.

The activities of superoxide dismutase (SOD) (E.C.1.15.1.1) in extracts of five cestode parasites (Moniezia expansa, M. benedeni, Avitellina centripunctata. Taenia hydatigena and Dipylidium caninum) were investigated. The polyacrylamide gel electrophoretic patterns revealed that each of the five species had four isoenzyme bands; they could be differentiated principally by their displacements and, less clearly, by their intensities. Determinations were made of the inhibitory activities of four benzimidazoles and six recently synthesised pyrimidine derivatives on the SOD enzymes from the cestodes. The results confirm that the percentage of inhibitions of SOD by the same pyrimidine derivatives are markedly superior to those of the benzimidazoles.