Malaria parasites adapt to the oxidative stress during their erythrocytic stages with the help of vital thioredoxin redox system and glutathione redox system. Glutathione reductase and thioredoxin reductase are important enzymes of these redox systems that help parasites to maintain an adequate intracellular redox environment. In the present study, activities of glutathione reductase and thioredoxin reductase were investigated in normal and Plasmodium berghei-infected mice red blood cells and their fractions. Activities of glutathione reductase and thioredoxin reductase in P. berghei-infected host erythrocytes were found to be higher than those in normal host cells. These enzymes were mainly confined to the cytosolic part of cell-free P. berghei. Full characterization and understanding of these enzymes may promise advances in chemotherapy of malaria.
Animals ; Antioxidants/*isolation & purification/*metabolism ; Cell Fractionation ; Cytosol/enzymology ; Erythrocytes/parasitology ; Glutathione Reductase/*isolation & purification/*metabolism ; Mice ; Plasmodium berghei/*enzymology ; Thioredoxin-Disulfide Reductase/*isolation & purification/*metabolism