L. Avilan et P. Garcia, HYSTERESIS OF CYTOSOLIC NADP-MALIC ENZYME II FROM TRYPANOSOMA-CRUZI, Molecular and biochemical parasitology, 65(2), 1994, pp. 225-232
NADP-malic enzyme II, one of two isoenzymes of NADP-malic enzyme (EC 1
.1.1.40) in Trypanosoma cruzi epimastigotes, presents hysteretic behav
ior that results in a kinetic lag in the reaction progress curve. The
lag is affected by the malate, aspartate and oxalacetate concentration
s in the assay mixture. This dependence suggests that hysteresis is du
e 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 in
volving column chromatography on DEAE-Sephacel and Cibacron-blue Sepha
rose. The molecular mass of the highly purified enzyme was determined
as 126 kDa.