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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2007-6-1
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pubmed:abstractText |
Nonenzymatic glycation of peptides and proteins by d-glucose has important implications in the pathogenesis of diabetes mellitus, particularly in the development of diabetic complications. However, no effective high-throughput methods exist for identifying proteins containing this low-abundance post-translational modification in bottom-up proteomic studies. In this report, phenylboronate affinity chromatography was used in a two-step enrichment scheme to selectively isolate first glycated proteins and then glycated, tryptic peptides from human serum glycated in vitro. Enriched peptides were subsequently analyzed by alternating electron-transfer dissociation (ETD) and collision induced dissociation (CID) tandem mass spectrometry. ETD fragmentation mode permitted identification of a significantly higher number of glycated peptides (87.6% of all identified peptides) versus CID mode (17.0% of all identified peptides), when utilizing enrichment on first the protein and then the peptide level. This study illustrates that phenylboronate affinity chromatography coupled with LC-MS/MS and using ETD as the fragmentation mode is an efficient approach for analysis of glycated proteins and may have broad application in studies of diabetes mellitus.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-11427445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-11525875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-12754519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-12754521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-14582647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-14641078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-15047055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-1505778,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-15210983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-15768376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-15822944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-15975085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-16037243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-16180244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-16887931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-17024709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-17063450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-17074749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-17125156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-17279487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-1907246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-2675036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-3071181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-3319287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-3568426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-3621595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-3753285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-4030761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-6712132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-7827091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-8514859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-8820792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17488106-9749578
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1535-3893
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2323-30
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pubmed:dateRevised |
2011-1-25
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pubmed:meshHeading |
pubmed-meshheading:17488106-Amino Acid Sequence,
pubmed-meshheading:17488106-Boronic Acids,
pubmed-meshheading:17488106-Chromatography, Affinity,
pubmed-meshheading:17488106-Electron Transport,
pubmed-meshheading:17488106-Glucose,
pubmed-meshheading:17488106-Glycopeptides,
pubmed-meshheading:17488106-Glycosylation,
pubmed-meshheading:17488106-Mass Spectrometry,
pubmed-meshheading:17488106-Molecular Sequence Data,
pubmed-meshheading:17488106-Proteomics
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pubmed:year |
2007
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pubmed:articleTitle |
Enrichment and analysis of nonenzymatically glycated peptides: boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry.
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pubmed:affiliation |
Biological Sciences Division and Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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