Bràz J, Lechner M C
FEBS Lett. 1986 Apr 21;199(2):164-8. doi: 10.1016/0014-5793(86)80472-0.
Changes in the ADP-ribosylation of total proteins and purified histones of rat liver nuclei after phenobarbital treatment (80 mg/kg, 24 h) have been studied. The [32P]NAD incorporation into total trichloroacetic acid precipitated proteins, in histone Hl and in core histones was evaluated, the specific radioactivities increasing 150, 40 and 8%, respectively. Histones Hl and H2B were the best ADP-ribose acceptors. Histone H4 did not show any 32P incorporation, as revealed by autoradiography after SDS-PAGE of the purified histones, in either the control or phenobarbital treated rats. Possible involvement of ADP-ribosylation of nuclear proteins in the adaptative response of liver to phenobarbital is discussed.
研究了苯巴比妥（80毫克/千克，24小时）处理后大鼠肝细胞核总蛋白和纯化组蛋白的ADP-核糖基化变化。评估了[32P]NAD掺入三氯乙酸沉淀的总蛋白、组蛋白H1和核心组蛋白中的情况，比放射性分别增加了150%、40%和8%。组蛋白H1和H2B是最佳的ADP-核糖受体。纯化组蛋白经SDS-PAGE后进行放射自显影显示，无论是对照大鼠还是经苯巴比妥处理的大鼠，组蛋白H4均未显示出任何32P掺入。讨论了核蛋白的ADP-核糖基化可能参与肝脏对苯巴比妥的适应性反应。
