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

Jie Zhang; Solomon H. Snyder

doi:10.1021/bi00060a014

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

Jie Zhang, Solomon H. Snyder

School of Medicine

Research output: Contribution to journal › Article › peer-review

35 Scopus citations

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)
Pages (from-to)	2228-2233
Number of pages	6
Journal	Biochemistry
Volume	32
Issue number	9
DOIs	https://doi.org/10.1021/bi00060a014
State	Published - 1993

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1021/bi00060a014

Cite this

@article{8e6bf149910e41969b956dba5b47e169,

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

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.",

author = "Jie Zhang and Snyder, {Solomon H.}",

year = "1993",

doi = "10.1021/bi00060a014",

language = "English (US)",

volume = "32",

pages = "2228--2233",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "9",

}

TY - JOUR

T1 - Purification of a Nitric Oxide-Stimulated ADP-Ribosylated Protein Using Biotinylated β-Nicotinamide Adenine Dinucleotide

AU - Zhang, Jie

AU - Snyder, Solomon H.

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0027394472&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027394472&partnerID=8YFLogxK

U2 - 10.1021/bi00060a014

DO - 10.1021/bi00060a014

M3 - Article

C2 - 8443164

AN - SCOPUS:0027394472

SN - 0006-2960

VL - 32

SP - 2228

EP - 2233

JO - Biochemistry

JF - Biochemistry

IS - 9

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this