Abstract
Abstract A simple and sensitive method for the assay of human erythrocyte hypoxanthine-guanine phosphoribosyltransferase (HG-PRTase) and adenine phosphoribosyltransferase (A-PRTase) activity is described in which separation of nucleotide from purine is achieved by ligand-exchange chromatography. The mean specific activity of HG-PRTase for normal individuals is 2.14 mμmoles per minute per milligram of protein with hypoxanthine as substrate and 2.49 mμmoles per minute per milligram of protein with guanine as substrate. Red blood cells from patients with the Lesch-Nyhan syndrome are not completely deficient in HG-PRTase activity but have approximately 2 per cent of the normal activity. The mean specific activity of A-PRTase in normal individuals is 0.431 mμmole per minute per milligram of protein while those of patients with the Lesch-Nyhan syndrome are doubled.
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