| Abstract: | 5-Phosphoribosyl-l-pyrophosphate, a substrate shared by adenine phosphoribosyltransferase and hypoxanthine-guanine phosphoribosyltransferase, accumulates in human erythrocytes lacking hypoxanthine-guanine phosphoribosyltransferase. 5-Phosphoribosyl-l-pyrophosphate added to purified adenine phosphoribosyltransferase stabilizes it against heat inactivation. The increased activity of adenine phosphoribosyltransferase seen in erythrocytes deficient in hypoxanthine-guanine phosphoribosyltransferase may result from substrate stabilization of this enzyme in vivo. |
