The Purine Phosphoribosyltransferases of Crithidia fasciculata

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Abstract
The purine phosphoribosyltransferases of C. fasciculata were identified and some of their properties described. The organism possesses 3 separate enzymes for the production of AMP, IMP and GMP. The evidence for this comes from the observed differences in elution patterns from gel filtration columns, differences in heat sensitivity, and especially the clear separation of hypoxanthine phosphoribosyltransferase (HPRTase) from guanine phosphoribosyltransferase [GPRTase] by affinity chromatography on GMP-agarose. APRTase [adenine phosphoribosyltransferase] is activated most efficiently by Zn2+, whereas HPRTase and GPRTase are activated most efficiently by Co2+. In no case did the product mononucleotides produce strong inhibition of the transferase activities.

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