Electrophoresis of glucose-6-phosphate and 6-phosphogluconate dehydrogenases in erythrocytes from malaria-infected animals.

Electrophoresis of red-cell extracts from control and malaria-infected animals on 'Cellogel' demonstrated the absence of G-6-PD activity of 'parasite' origin, although 6-PGD activity was present. An identical 6-PGD isoenzyme was found in mice, rats and hamsters infected with the same strain of Plasmodium berghei indicating the parasite as the source of the enzyme. A similar 6-PGD isoenzyme was also found in a few preliminary experiments with P. knowlesi-infected monkey erythrocytes. The implications of these findings are discussed in relation to previous studies and also to the status of the pentose phosphate pathway in plasmodial metabolism.