Hers H G, Van Den Berghe G
Lancet. 1979 Mar 17;1(8116):585-6. doi: 10.1016/s0140-6736(79)91010-9.
The rate-limiting step in the degradation of adenine nucleotides in the liver is the conversion of adenosine monophosphate (A.M.P.) to inosine monophosphate by A.M.P. deaminase, which is normally 95% inhibited. When the inhibition is released, uric acid is formed in large excess, and the biosynthesis of purines is increased. We therefore propose that congenital hyperuricaemia is caused by the presence of an abnormal A.M.P. deaminase, which is less sensitive to its physiological inhibitors. Verification of the hypothesis depends upon the availability of liver tissue from patients with congenital hyperuricaemia for kinetic analysis of A.M.P. deaminase. A call for collaboration is addressed to the medical community.
肝脏中腺嘌呤核苷酸降解的限速步骤是单磷酸腺苷（A.M.P.）通过A.M.P.脱氨酶转化为单磷酸肌苷，该过程通常受到95%的抑制。当这种抑制作用解除时，尿酸会大量生成，同时嘌呤的生物合成会增加。因此，我们推测先天性高尿酸血症是由异常的A.M.P.脱氨酶导致的，这种脱氨酶对其生理抑制剂的敏感性较低。该假说的验证取决于能否获取先天性高尿酸血症患者的肝脏组织，以对A.M.P.脱氨酶进行动力学分析。我们呼吁医学界展开合作。
