Abstract
The agent of avian malaria, Plasmodium lophurae, contains an NADP-glutamate dehydrogenase (EC 1.4.1.2) which is capable of oxidizing glutamate to α-ketoglutarate. This glutamate dehydrogenase exists as a single electrophoretic form in both the free parasite and in the malaria-infected cell; the normal erythrocyte contains two other electrophoretic forms of low activity. It is suggested that the oxidation of glutamate, and its further metabolism via the Krebs tricarboxylic acid cycle may provide an additional energy source for the parasite.
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