STABILIZATION AND CHARACTERIZATION OF PHOSPHOFRUCTOKINASE PURIFIED FROM SETARIA-CERVI, A BOVINE FILARIAL PARASITE

Phosphofructokinase (ATP:D-fructose-6-phosphate-1-phosphotransferase, PFK) (EC 2.7.1.11) was isolated from cytosolic fraction of adults (mal e/female) and microfilarial (Mf) stages of Setaria cervi, a bovine fil arial worm. The activity of purified enzyme was stable in the presence of aforesaid factors (minus ethanol) for about 10 days. The purified enzyme preparation showed a single protein band on polyacrylamide gel electrophoresis under non-reducing conditions. The molecular weight of the enzyme as determined by gel filtration through Sephadex G-150 was about 180,000. S. cervi PFK was highly thermolabile and exhibited two pH optima depending on ATP concentrations. The enzyme showed wide spe cificity to divalent cations, prefering Mg2+ over other metal ions. Th e filarial PFK was different from the analogous enzyme of mammalian an d other organisms in certain characteristic properties as discussed.