Richter C, Winterhalter K H, Baumhüter S, Lötscher H R, Moser B
Proc Natl Acad Sci U S A. 1983 Jun;80(11):3188-92. doi: 10.1073/pnas.80.11.3188.
NAD+ glycohydrolase activity is found at high levels in submitochondrial particles. It leads to the reaction products ADP-ribose, nicotinamide, and small amounts of 5'-AMP. Furthermore, submitochondrial particles catalyze the exchange reaction: [adenosine-14C]ADP-ribose + NAD+ in equilibrium [adenosine-14C]-NAD+ + ADP-ribose. When submitochondrial particles are incubated with NAD+, mono(ADP-ribosyl)ation of protein molecules migrating with an apparent molecular weight of 30,000 in sodium dodecyl sulfate/polyacrylamide gel electrophoresis is demonstrable. Inhibitor studies suggest attachment of ADP-ribose to arginine residues. ADP-ribose bound to submitochondrial particles is rapidly turning over. The release of ADP-ribose from the protein is probably enzyme catalyzed. The rapid turnover, the specificity of the modification, and the inhibition of ADP-ribosylation by ATP and nicotinamide suggest a regulatory role of mono(ADP-ribosyl)ation of a protein in the inner mitochondrial membrane.
在线粒体亚颗粒中发现了高水平的NAD + 糖水解酶活性。它会产生反应产物ADP-核糖、烟酰胺和少量的5'-AMP。此外，线粒体亚颗粒催化交换反应：[腺苷-14C]ADP-核糖 + NAD + 处于平衡状态 [腺苷-14C]-NAD + + ADP-核糖。当线粒体亚颗粒与NAD + 一起孵育时，在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳中可证明表观分子量为30,000的蛋白质分子发生了单（ADP-核糖基）化。抑制剂研究表明ADP-核糖与精氨酸残基相连。与线粒体亚颗粒结合的ADP-核糖迅速周转。ADP-核糖从蛋白质上的释放可能是酶催化的。快速周转、修饰的特异性以及ATP和烟酰胺对ADP-核糖基化的抑制表明线粒体内膜中蛋白质的单（ADP-核糖基）化具有调节作用。
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