PURIFICATION AND CHARACTERIZATION OF DNA-POLYMERASES FROM PLASMODIUM-FALCIPARUM

Fractionation of Plasmodium falciparum cellular extracts by fast prote in liquid chromatography (FPLC) identified at least two different DNA polymerases. An aphidicolin-sensitive activity co-purified with a prim ase activity. This, in combination with other characteristics (process ivity, sensitivity to other inhibitors), most likely classifies this e nzyme as an alpha-like DNA polymerase. It was, however, relatively res istant to N2-(p-n-butylphenyl)deoxyguanosine 5'-triphosphate (IC50 = 6 .6 muM) and differs in this aspect from the host homologue, possibly i ndicating structural differences between host and parasite DNA polymer ase alpha. The other DNA polymerase matched eukaryotic DNA polymerase gamma in all properties tested.