Poirier G G, Savard P
Can J Biochem. 1980 Jun;58(6):509-15. doi: 10.1139/o80-069.
Incubation of pancreatic nuclei with high NAD concentrations resulted in increased ADP-ribosylation of histone H1. Interaction of [3H]ADP-ribosylated histone H1 with chromatin was significantly different from unmodified histone H1. The presence of a protein which is eluted at a lower salt concentration and which is ADP-ribosylated was also noticed. Pancreatic histones were isolated by column chromatography and their degree of ADP-ribosylation evaluated both by gel electrophoresis and by chromatography: histone H1 was the main acceptor while the core histones H3, H2B, and H2A were lightly labelled. Histones H1 and H1(0) have a differential binding to pancreatic chromatin and histone H1(0) is not ADP-ribosylated.
用高浓度烟酰胺腺嘌呤二核苷酸（NAD）孵育胰腺细胞核会导致组蛋白H1的ADP核糖基化增加。[3H]ADP核糖基化组蛋白H1与染色质的相互作用与未修饰的组蛋白H1显著不同。还注意到存在一种在较低盐浓度下洗脱且被ADP核糖基化的蛋白质。通过柱色谱法分离胰腺组蛋白，并通过凝胶电泳和色谱法评估其ADP核糖基化程度：组蛋白H1是主要的受体，而核心组蛋白H3、H2B和H2A标记较轻。组蛋白H1和H1(0)与胰腺染色质有不同的结合，且组蛋白H1(0)未被ADP核糖基化。
