Partial purification and characterization of a murine malaria parasite, Plasmodium berghei specific aldolase

Cell-free P. berghei contains 26.1 times more aldolase activity as compared to normal mouse erythrocytes. Subcellular fractionation of cell-free parasite showed maximum enzyme activity in the soluble fraction. The parasite enzyme was active in a narrow pH range of 7.8-8.0. Of the enzyme activity 90% was lost within 2 weeks at 4 degrees C. Slight inhibition was observed with specific inhibitors ATP, pyrophosphate (PPi) and PEP. The F1, 6DP Km was 0.025 mM.