Abstract
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 H1 and in core histones was evaluated, the specific radioactivities increasing 150, 40 and 8%, respectively. Histones H1 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.
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