Selective enrichment of glycopeptides from glycoprotein digests using ion-pairing normal-phase liquid chromatography: Anal.Chem.

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TypeArticle
Journal titleAnal.Chem.
Volume79
Issue23
Pages88918899; # of pages: 9
Subjectanalysis; Canada; Chromatography; complex; COMPLEXES; DIFFERENCE; EFFICIENT; ENERGY; glycopeptide; Glycopeptides; glycoprotein; Glycoproteins; ISOLATION; method; Methods; Mixture; peptide; Peptides; protein; selective; STRUCTURAL; structural analysis; STRUCTURAL-ANALYSIS
AbstractDetailed structural analysis of glycoproteins requires methods capable of isolating glycopeptides from tryptic digests of purified glycoproteins and complex protein mixtures. Here, we describe the selective and reproducible isolation of glycopeptides from a peptide mixture using ion-pairing normal-phase chromatography (IP-NPLC). The addition of inorganic monovalent ions in normal-phase chromatography appears to increase the hydrophobicity difference between peptides and glycopeptides, allowing for more efficient separation. Our data show that IP-NPLC effectively enriches glycopeptides from a tryptic digest of ribonuclease B, bovine fetuin, and a complex mixture of glycoproteins, when compared with normal-phase chromatography alone. The results of the IP-NPLC experiments can be explained using the Wimley-White water/octanol free energy scale to illustrate the hydrophobicity difference of nonglycosylated peptides with and without ion-pairing. We believe that IP-NPLC will be an important tool in glycoprotein characterization and glycoproteomic studies
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberDING2007A
NPARC number9365159
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Record identifier2341b5a1-c59f-4f9d-ac49-15e14a46f448
Record created2009-07-10
Record modified2016-05-09
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