Purine base transport in normal and mutant erythrocytes.
The uptake of adenine and hypoxanthine in HGPRT-deficient and normal human erythrocytes was measured using a rapid filtering centrifugation technique. The transport of hypoxanthine as well as of adenine is impaired in the mutant cells. The transport of hypoxanthine into HGPRT-deficient erythrocytes differs from that into normal cells with respect to a higher accumulation capacity, to lower initial velocities and to the kinetic properties of the translocator. In addition, a higher accumulation capacity and lower initial velocities of adenine uptake could be demonstrated in  mutant cells. A linkage of the purine translocator with purine phosphoribosyltransferases associated with the erythrocyte membrane is discussed.
D000225:Adenine / Q000097:blood*; D004912:Erythrocytes / Q000201:enzymology / Q000378:metabolism*; D006073:Gout / Q000097:blood / Q000201:enzymology / Q000235:genetics; D006801:Humans; D007041:Hypoxanthine Phosphoribosyltransferase / Q000097:blood; D007042:Hypoxanthines / Q000097:blood*; D007926:Lesch-Nyhan Syndrome / Q000097:blood / Q000201:enzymology; D009154:Mutation; D013997:Time Factors
D007042:Hypoxanthines; D007041:Hypoxanthine Phosphoribosyltransferase; D000225:Adenine