Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-5-30
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
199
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
164-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
ADP-ribosylation of nuclear proteins is increased by phenobarbital. Identification of the ADP-ribosylated histone fractions in rat liver nuclei.
pubmed:publicationType
Journal Article