Purification of a Nitric Oxide-Stimulated ADP-Ribosylated Protein Using Biotinylated β-Nicotinamide Adenine Dinucleotide

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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 languageEnglish (US)
Pages (from-to)2228-2233
Number of pages6
JournalBiochemistry
Volume32
Issue number9
DOIs
StatePublished - 1993

ASJC Scopus subject areas

  • Biochemistry

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