Abstract
ERYTHROCYTIC stages of the malarial parasite apparently obtain the bulk of their amino acids from digestion of host cell haemoglobin1–5. In addition, intracellular degradation of unnecessary organelles occurs within the parasite following invasion of the host cell. Thus, it is rather surprising that there have been relatively few studies on the proteolytic enzymes of Plasmodium, since these would presumably be involved in both processes. Cell-free extracts of P. gallinaceum degraded denatured globin at pH 6.5, while haemoglobin was digested very slowly6. Data of Cook et al.7 indicate the existence of two proteinases, with pH optima of 4 and 8 (P. berghei) and 5 and 8 (P. knowlesi). In each case, the alkaline protease was the more active.
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LEVY, M., SIDDIQUI, W. & CHOU, S. Acid Protease Activity in Plasmodium falciparum and P. knowlesi and Ghosts of Their Respective Host Red Cells. Nature 247, 546–549 (1974). https://doi.org/10.1038/247546a0
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DOI: https://doi.org/10.1038/247546a0
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