LDH (Plasmodium falciparum)
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|Purity Confirmation||> 85% by SDS-PAGE & Coomassie stain|
|Molecular Weight||35 kDa|
|Buffer||50 mM Tris, 250 mM NaCl, 1 mM EDTA|
|Stability and Storage||According to the available data the liquid protein stored at 4-8°C is stable at least for about 10 months.|
|Description||Malaria is one of the most widespread infectious diseases affecting some 500 million people with an enormous cost in human suffering and economic hardship. Effective treatment of the disease is increasingly compromised by rising resistance of malaria parasites to currently available anti-malarials. The parasites are homolactate fermenters and rely on glycolysis for energy generation since the parasites appear to lack a functional citric acid cycle. The NAD+ consumed during glycolysis is reduced to NADH by lactate which, in turn, is oxidized to pyruvate. This reaction is catalyzed by lactate dehydrogenase (LDH). It has been demonstrated that inhibitors of this enzyme have parasiticidal activity. Since LDH from the malaria parasite Plasmodium falciparum (PfLDH) has notable structural and kinetic differences from human LDHs, the enzyme appears to be an attractive target for novel anti-malarial therapeutics. The parasite, P. falciparum, is the most lethal of malarial plasmodia being responsible for the cerebral form of the disease; consequently it has been the major focus of initial biochemical and genomic investigation. On the other hand, the parasite P. vivax is of great importance as it is the most widespread and common of the malarial plasmodia and, therefore, is responsible for the greatest burden of disease.|
- Quantification of malaria antigens PfHRP2 and pLDH by quantitative suspension array technology in whole blood, dried blood spot and plasma. X. Martiáñez-Vendrell et al., Malar J. 2020 Jan 9;19(1):12.
- Analytical sensitivity of current best-in-class malaria rapid diagnostic tests. A. Jimenez et al., Malar J. 2017; 16: 128.
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