Schultz V, Lowenstein J M
J Biol Chem. 1976 Jan 25;251(2):485-92.
Cell-free extracts of rat brain catalyze the reactions of the purine nucleotide cycle. Ammonia is formed during the deamination but not the amination phase of the cycle. The activity of adenylate deaminase in brain is sufficient to account for the maximum rates of ammonia production that have been reported. The activity of glutamate dehydrogenase is not sufficient to account for these rates of ammonia production. The activities of adenylosuccinate synthetase and adenylosuccinase are nearly sufficient to account for the steady state rates of ammonia production observed in brain. Demonstration of the cycle in extracts of brain is complicated by the occurrence of side reactions, in particular those catalyzed by phosphomonoesterase, nucleoside phosphorylase, and guanase.
大鼠脑的无细胞提取物可催化嘌呤核苷酸循环的反应。在循环的脱氨基阶段而非氨基化阶段会生成氨。脑中腺苷酸脱氨酶的活性足以解释已报道的最大氨生成速率。谷氨酸脱氢酶的活性不足以解释这些氨生成速率。腺苷酸琥珀酸合成酶和腺苷酸琥珀酸酶的活性几乎足以解释脑中观察到的氨生成稳态速率。脑中提取物中该循环的证明因副反应的发生而变得复杂,尤其是由磷酸单酯酶、核苷磷酸化酶和鸟嘌呤酶催化的那些反应。