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Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.

Abstract：

:A selective method for the enrichment of O-GlcNAcylated peptides using a novel CLICK chemistry reagent is described. Peptides modified by O-GlcNAc were enzymatically labeled with N-azidoacetylgalactosamine. The azide was then reacted with a phospho-alkyne using CLICK chemistry and O-GlcNAcGalNAzPO(4)-containing peptides were enriched using titanium dioxide chromatography. Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment. The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells. A total of 42 unique O-GlcNAcylated peptides were identified, including 7 novel O-GlcNAc sites.

journal_name

J Proteome Res

journal_title

Journal of proteome research

authors

Parker BL,Gupta P,Cordwell SJ,Larsen MR,Palmisano G

doi

10.1021/pr100565j

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

1449-58

issue

4

eissn

1535-3893

issn

1535-3907

journal_volume

10

pub_type

杂志文章

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