Characterization of the enhanced transport of L- and D-lactate into human red blood cells infected with Plasmodium falciparum suggests the presence of a novel saturable lactate proton cotransporter.

@article{Cranmer1995CharacterizationOT,
  title={Characterization of the enhanced transport of L- and D-lactate into human red blood cells infected with Plasmodium falciparum suggests the presence of a novel saturable lactate proton cotransporter.},
  author={Susan L. Cranmer and Alan R. Conant and Winston Edward Gutteridge and Andrew Philip Halestrap},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 25},
  pages={
          15045-52
        }
}
Human erythrocytes parasitized with the malarial protozoan Plasmodium falciparum showed rates of L-lactate, D-lactate, and pyruvate uptake many fold greater than control cells. Thus it was necessary to work at 0 degrees C to resolve true initial rates of transport. Studies on the dependence of the rate of transport on substrate concentration implied the presence in parasitized cells of both a saturable mechanism blocked by alpha-cyano-4-hydroxycinnamate (CHC) and a nonsaturable mechanism… CONTINUE READING
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