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J Parasitol. 1980 Apr;66(2):205-12.

Purine base and nucleoside uptake in Plasmodium berghei and host erythrocytes.


The absorption of 3H-labeled adenine, adenosine, hypoxanthine, and 14C-labeled inosine by normal rat erythrocytes, Plasmodium bergheri-infected erythrocytes and saponin released "free parasites" was measured. The uptake of these labeled substrates by normal rat erythrocytes occurs both by diffusion and mediated transport systems. Similar absorptive mechanisms for these substrates also were observed for both Plasmodium berghei-infected erythrocytes and "free parasites." Data from inhibition studies using purine base and nucleoside analogues indicate the presence of three distinct transport loci in the normal erythrocyte for adenosine-inosine, hypoxanthine, and adenine and two loci in the infected erythrocyte and "free parasite" for adenosine-inosine-hypoxanthine and adenine. The initial metabolism of 3H-adenosine by the "free parasite" also was examined. A double isotope technique was used to follow the separate metabolic fates of the purine base and ribose moieties of adenosine. The data suggest a possible conversion of adenosine to the purine base and ribose moiety and subsequent uptake of the purine base by the parasite. In addition, a powerful adenosine deaminase inhibitor (2-deoxcoformycin) significantly reduced the uptake of 3H-adenosine by the "free parasites." Chromatographs of aliquots from postincubation media show the tritium label to be associated predominately with adenosine in the presence of 2-deoxycoformycin and with isoine and hypoxanthine in the absence of the inhibitor.

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