Hysteresis of cytosolic NADP-malic enzyme II from Trypanosoma cruzi

Luisana Avilán, Pablo García

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)225-32
Number of pages8
JournalMolecular and Biochemical Parasitology
Volume65
Issue number2
DOIs
Publication statusPublished - Jun 1994

Keywords

  • Animals
  • Cytosol/enzymology
  • Malate Dehydrogenase/analysis
  • Trypanosoma cruzi/enzymology

Fingerprint

Dive into the research topics of 'Hysteresis of cytosolic NADP-malic enzyme II from <i>Trypanosoma cruzi</i>'. Together they form a unique fingerprint.

Cite this