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The heterogeneity of erythrocyte IMP: pyrophosphate phosphoribosyl transferase and purine nucleoside phosphorylase by isoelectric focusing

M. Davies,B. Dean

Published 1971 in FEBS Letters

ABSTRACT

The recent demonstration that human erythrocyte IMP:pyrophosphate phosphoribosyl transferase (HxPRTase) has properties compatible with it being subject to allosteric regulation [ 1 ] has raised the possibility of the existence of subunits in this enzyme. The structural gene for HxPRTase is believed to be X-linked, but no variant of the human red cell enzyme was detected in 382 blood samples examined by electrophoresis in starch gel [2] . Four isoenzymes of HxPRTase have, however, been demonstrated by Bakay and Nyhan [3] using columns of polyacrylamide gel and a partially purified enzyme preparation from human erythrocytes. We wish to report here the results of some isoelectric focusing experiments which clearly demonstrate the heterogeneity of this enzyme in haemolysed human erythrocytes, and which also suggest an inter-relationship between this enzyme controlling the conversion of hypoxanthlne to IMP and the enzyme purine nucleoside phosphorylase (NP) which converts hypoxanthine to inosine.

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