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Measurement of the Lactate Dehydrogenase Activity of Plasmodium falciparum as an Assessment of Parasitemia

American Journal of Tropical Medicine and Hygiene · 1993 · Vol. 48(2) · pp. 205–210
Michael T. MaklerDavid J. Hinrichs

Abstract

This report describes an enzyme assay for the detection of Plasmodium falciparum. The assay is based on the observation that the lactate dehydrogenase (LDH) enzyme of P. falciparum has the ability to rapidly use 3-acetyl pyridine NAD (APAD) as a coenzyme in the reaction leading to the formation of pyruvate from lactate. Human red blood cell LDH carries out this reaction at a very slow rate in the presence of APAD. We measured the development of APADH and found that the formation of this product could establish the basis of an assay that detected the presence of P. falciparum from in vitro cultures at parasitemia levels of 0.02%. We also had occasion to use this assay with clinical samples. We found a correlation between levels of parasitemia and the activity of parasite LDH. Parasite LDH (pLDH) activity could be measured in blood hemolysates and in plasma and serum from patients with malaria. We used the serum assay for pLDH and followed the level of pLDH in a patient with cerebral malaria prior to antimalarial treatment and during the recovery period. From these initial studies, it is evident that the measurement of pLDH has a correlation with parasitemia and may offer a method that can be developed into a simple test for the detection of Plasmodium parasitemia.

Malaria Research and ControlHIV/AIDS drug development and treatmentParasitemiaLactate dehydrogenasePlasmodium falciparumMalariaParasite hostingBiologyHemoglobinEnzymeBiochemistryChemistry

MeSH terms

AnimalsErythrocytesHumansIsoenzymesL-Lactate DehydrogenasePlasmodium falciparumSpectrophotometryMalaria, Falciparum
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