Abstract
ADP-ribosylation, involving the transfer of an ADP-ribose moiety from NAD to proteins, is mediated by several bacterial toxins and endogenous ADP-ribosyltransferases. We report here the synthesis of biotinylated NAD and its use to label and purify biotinyl-ADP-ribosylated proteins. We demonstrate that biotinylated NAD can be used by diphtheria toxin to biotinylate elongation factor 2. Using avidin affinity chromatography, we have purified a protein whose ADP-ribosylation is enhanced by nitric oxide and which has been identified as glyceraldehyde-3-phosphate dehydrogenase.
Original language | English (US) |
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Pages (from-to) | 2228-2233 |
Number of pages | 6 |
Journal | Biochemistry |
Volume | 32 |
Issue number | 9 |
DOIs | |
State | Published - 1993 |
ASJC Scopus subject areas
- Biochemistry