ADP-ribosylation of diadenosine 5',5"-P1,P4-tetraphosphate by poly(ADP-ribose) polymerase in vitro.
作者： K. Yoshihara , Y. Tanaka
DOI: 10.1016/S0021-9258(19)69056-3
关键词:
摘要: Abstract When the effect of diadenosine 5',5"'-P1,P4-tetraphosphate on a purified poly(ADP-ribose) polymerase reaction was examined, compound strongly inhibited ADP-ribosylation histone, while much less inhibitory Mg2+-dependent automodification this enzyme. In an attempt to study mechanism inhibition, we analyzed total products, which were synthesized from NAD+ in presence mixture for and found that new, low molecular product predominantly instead ADP-ribosylated histone reaction. Approximately 90% added converted into under appropriate condition. Further analysis revealed mono- oligo(ADP-ribosyl)ated nucleotide bound oligo(ADP-ribose) is elongating at one end during Thus, present clearly demonstrated functions as acceptor ADP-ribose vitro. The finding H1 required synthesis new suggests interact modification
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