Riccio P, Simone S M, Passarella S, Marra E, Quagliariello E
Boll Soc Ital Biol Sper. 1979 Dec 15;55(23):2419-24.
The present work is an extension of our precedent papers (1-3). In the present report the relationship was studied between the inhibition by 3H-NQNO, 3-3H-2-n-nonyl-4-hydroxy-quinoline-N-oxide, of the respiratory activity induced in submitochondrial particles from beef heart by NADH and the binding of 3H-NQNO to the specific binding site. The experiments showed that the concentrations of inhibition sites and of specific binding sites are identical. Titrating the inhibition of NADH-oxidase activity with increasing amounts of 3H-NQNO a close connection was observed between the decrease of the respiratory activity and the increase of the specific binding of 3H-NQNO. When nearly full inhibition (85%) was reached, also the specific binding was saturated. We may conclude that 3H-NQNO behaves like an ideally simple inhibitor: the inhibition of electron transfer by 3H-NQNO is linear with the saturation of the specific binding site.
本研究是我们之前论文（1 - 3）的扩展。在本报告中，研究了3H - NQNO（3 - 3H - 2 - 正壬基 - 4 - 羟基喹啉 - N - 氧化物）对牛心亚线粒体颗粒中由NADH诱导的呼吸活性的抑制作用与3H - NQNO与特异性结合位点的结合之间的关系。实验表明，抑制位点和特异性结合位点的浓度是相同的。用增加量的3H - NQNO滴定NADH氧化酶活性的抑制作用时，观察到呼吸活性的降低与3H - NQNO特异性结合的增加之间存在密切联系。当达到几乎完全抑制（85%）时，特异性结合也达到饱和。我们可以得出结论，3H - NQNO表现得像一种理想的简单抑制剂：3H - NQNO对电子传递的抑制作用与特异性结合位点的饱和呈线性关系。
