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- W2021199616 abstract "Besides its function as a major electon acceptor, NAD is a substrate for numerous ADP-ribose transfer reactions that are important in the regulation of cell function. The poly(ADP-ribosyl)ation of nuclear proteins has been shown to modify chromatin structure. The mono(ADP-ribosyl)ation of elongation factor-2, catalyzed by diphtheria and psuedomonas toxins, has been demonstrated to block protein synthesis. The mono(ADP-ribosyl)ation of G proteins by bacterial toxins can critically modulate transmembrane signalling. We have developed a simple method to distinguish between mono(ADP-ribosyl)ation and poly(ADP-ribosyl)ation reactions in crude cell extracts. Radioactive 2′-deoxyNAD (dNAD) was prepared enzymatically from [2,8-3H]-dATP and nicotinamide mononucleotide, and was purified by HPLC. Then dNAD and NAD were compared as substrates for purified poly(ADP-ribose) polymerase from calf spleen, and diphtheria toxin mono(ADP-ribose) transferase. The results showed that 2′-dNAD was an efficient substrate for the mono(ADP-ribose) transferase. The transfer of the dADP moiety of dNAD to elongation factor-2 inhibited protein synthesis in reticulocyte lysates. In contrast, dNAD was not a detectable substrate for poly(ADP-ribose) polymerase, under conditions where NAD was rapidly consumed. These results suggest that dNAD may be a useful tool for the investigation of specific cellular targets of eukaryotic and bacterial mono(ADP-ribosyl)ation reactions." @default.
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- W2021199616 date "1988-07-01" @default.
- W2021199616 modified "2023-09-26" @default.
- W2021199616 title "171 UTILIZATION OF 2′-DEOXYNAD FOR ADP-RIBOSE TRANSFER REACTIONS" @default.
- W2021199616 doi "https://doi.org/10.1203/00006450-198807000-00195" @default.
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