Plasmodium berghei: Glycolytic enzymes of the infected mouse erythrocyte |
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Authors: | Walter C. Kruckeberg Barry J. Sander Donna C. Sullivan |
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Affiliation: | University of Mississippi Medical Center, Department of Preventive Medicine, 2500 North State Street, Jackson, Mississippi 39216, U.S.A. |
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Abstract: | This paper documents the maximal activities of the glycolytic enzymes in the red blood cells of normal mice and mice infected with Plasmodium berghei. There appears to be sufficient parasite-related activity of each glycolytic enzyme to support the increased glycolytic rate, i.e., increased glucose consumption, of the parasite-infected red blood cell. The relative proportions of glycolytic enzyme activities in parasite-infected red cells are different from the proportions in either normal or reticulocyte-rich blood, indicating that the increased enzyme activities associated with infected cells are not due to contaminating host red cells or reticulocytes. A comparison of maximal enzyme activities to the rate of whole cell glucose consumption indicates that different glycolytic control mechanisms are operating in the infected RBC from those in the uninfected cells. |
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Keywords: | Malaria, rodent Protozoa, parasitic Glycolytic metabolism Glycolytic enzymes Mouse Erythrocyte Glucose consumption Intra-cellular pH Reticulocytosis HK hexokinase GPI glucose phosphate isomerase PFK phosphofructokinase Aid aldolase TPI triosephosphate isomerase GAPD glyceraldehyde-3-phosphate dehydrogenase DPGM diphosphoglycerate mutase PFK phosphoglycerate kinase PGlyM phosphoglycerate mutase Enol enolase PK pyruvate kinase LDH lactate dehydrogenase G6PD glucose-6-phosphate dehydrogenase 6PGD 6-Dhosohoeluconate dehvdroeenase |
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