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Purine Phosphoribosyl Transferases in Human Erythrocyte Ghosts

  • C. H. M. M. de Bruyn
  • T. L. Oei
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Part of the Advances in Experimental Medicine and Biology book series

Abstract

It is generally assumed that mammalian hypoxanthine-guanine phosphoribosyl transferase (HG-PRT; EC 2.4.2.8) and adenine phosphoribosyl transferase (A-PRT; EC 2.4.2.7) are soluble, cytoplasmic enzymes. All the isolation procedures for these enzymes are based on purification from cell free supernatant fractions (1–6). Little attention has been paid to the subcellular localisation of purine phosphoribosyl transferases. With respect to isolated cell membranes it has been reported that human erythrocyte and fibroblast membranes do not display HG-PRT activity (7).

Keywords

Erythrocyte Ghost Phosphoribosyl Transferase Isolate Cell Membrane Intact Erythrocyte Adenine Phosphoribosyl Transferase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • C. H. M. M. de Bruyn
    • 1
  • T. L. Oei
    • 1
  1. 1.Dept. Hum. GeneticsUniversity of NijmegenThe Netherlands

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