Abstract
NADP-malic enzyme II, one of two isoenzymes of NADP-malic enzyme (EC 1.1.1.40) in Trypanosoma cruzi epimastigotes, presents hysteretic behavior that results in a kinetic lag in the reaction progress curve. The lag is affected by the malate, aspartate and oxaloacetate concentrations in the assay mixture. This dependence suggests that hysteresis is due to an association-dissociation process influenced by the binding of these ligands to the enzyme. The enzyme was separated from NADP-malic enzyme I and purified 43-fold from a cell homogenate by a procedure involving column chromatography on DEAE-Sephacel and Cibacron-blue Sepharose. The molecular mass of the highly purified enzyme was determined as 126 kDa.
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