Masmoudi A, Mandel P
Biochemistry. 1987 Apr 7;26(7):1965-9. doi: 10.1021/bi00381a027.
ADP-ribosyl transferase and NAD glycohydrolase activities have been estimated in mitochondria in mitoplasts as well as in other submitochondrial fractions. A high activity of these two enzymes was present in mitoplasts as compared to the outer membrane preparation or intermembrane compartment. Inhibitor studies provide strong evidence for the involvement of ADP-ribosyl transferase in the process of ADP-ribosylation of mitochondrial proteins. When NAD glycohydrolase was blocked by nicotinamide or 3-aminobenzamide, the incorporation of ADP-ribose into mitochondrial proteins still occurs. ADP-ribosyl transferase activity could also be detected when NAD glycohydrolase was separated by hydroxylapatite chromatography. The protein-linked ADP-ribose moiety appears to be an oligomer in mitochondria.
已对线粒体、线粒体小体以及其他亚线粒体组分中的ADP-核糖基转移酶和NAD糖水解酶活性进行了评估。与外膜制剂或膜间腔相比，线粒体小体中这两种酶的活性较高。抑制剂研究为ADP-核糖基转移酶参与线粒体蛋白的ADP-核糖基化过程提供了有力证据。当NAD糖水解酶被烟酰胺或3-氨基苯甲酰胺阻断时，ADP-核糖仍会掺入线粒体蛋白中。当通过羟基磷灰石色谱法分离NAD糖水解酶时，也能检测到ADP-核糖基转移酶活性。蛋白质连接的ADP-核糖部分在线粒体中似乎是一种寡聚物。
