Abstract
Two enzymes from Plasmodium falciparum that catalyze the formation of NADPH have been partially purified and characterized. Glutamate dehydrogenase (GDH), molecular mass 230 Kd, pH optimum 7.0, is capable of producing NADPH under optimum conditions at about 10% of the capacity of the host erythrocyte. This capacity increases slightly during the developmental cycle of the parasite. NADP-specific isocitrate dehydrogenase (IDH), molecular mass 80 Kd, pH optimum 7.5, is capable of producing NADPH at 20% to 60% of the capacity of the host cell, depending on the developmental stage of the parasite. Increasing IDH activity is observed as the parasite matures. GDH and IDH provide the parasite with NADPH-generating abilities that compare favorably with the host cell.
