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).
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© 1977 Plenum Press, New York
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de Bruyn, C.H.M.M., Oei, T.L. (1977). Purine Phosphoribosyl Transferases in Human Erythrocyte Ghosts. In: Müller, M.M., Kaiser, E., Seegmiller, J.E. (eds) Purine Metabolism in Man—II. Advances in Experimental Medicine and Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-4223-6_18
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DOI: https://doi.org/10.1007/978-1-4613-4223-6_18
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