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.
D000818:Animals; D006224:Cricetinae; D004588:Electrophoresis, Cellulose Acetate; D004912:Erythrocytes / Q000201:enzymology*; D005954:Glucosephosphate Dehydrogenase / Q000097:blood*; D000882:Haplorhini; D006454:Hemoglobins / Q000032:analysis; D008253:Macaca mulatta; D008288:Malaria / Q000201:enzymology*; D051379:Mice; D010734:Phosphogluconate Dehydrogenase / Q000097:blood*; D010962:Plasmodium berghei; D051381:Rats
D006454:Hemoglobins; D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase