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Title: Purification of a nitric oxide-stimulated ADP-ribosylated protein using biotinylated beta-nicotinamide adenine dinucleotide. Author: Zhang J, Snyder SH. Journal: Biochemistry; 1993 Mar 09; 32(9):2228-33. PubMed ID: 8443164. 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.[Abstract] [Full Text] [Related] [New Search]