[Pyruvate kinase from Calicophoron ijimai trematodes and its potential inhibition by anthelmintic preparations].

It was shown that pyruvate kinase (PK) in the supernatant fraction from Calicophoron ijimai is able to regulate the direction of metabolic flow at glucose break down from phosphoenolpyruvate (PEP) level. The enzyme for activity required substrate, dinucleotides, cations K+ and Mn++. The activity with Mg++ as divalent cation is low. The addition of fructose-1.6-diphosphate (FDP) did not affect the enzyme activity with Mn++, however, increased the affinity for PEP. The velocity of Mg++ activated reaction increased by 8.2 times in the presence of FDP. PK in C. ijimai is sensitive to ATP inhibition, being weakly inhibited by malate. L-alanine did not influence on the enzyme activity. The effect of some anthelminthic preparations on the PK activity was shown.