کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1205409 | 965195 | 2008 | 6 صفحه PDF | دانلود رایگان |
We describe a new capillary electrophoresis–mass spectrometry (CE–MS)-based technique for analyzing sulfated glycopeptides. The proposed method performs selective enrichment of sulfated glycopeptides from a complex mixture of peptides based on field-enhanced sample injection and ion-pair reaction with a basic ion-pair reagent (Lys-Lys-Lys; KKK) at the exit end of a capillary in a single analysis, which permits successful fragmentation of sulfated glycopeptides in positive-ion mode at the MS/MS stage for comprehensive structural analysis. In this study, the method was verified using a model sulfated monosaccharide, N-acetyl-d-galactosamine 4-sulfate (GalNAc 4S). As an example of an application of this method, sulfated glycopeptides were selectively enriched from the enzymatic digest of thyroid stimulating hormone, affording ∼500-fold sensitivity enhancement, and structural information was successfully obtained via on-line ion-pair complexation reaction.
Journal: Journal of Chromatography A - Volume 1194, Issue 2, 20 June 2008, Pages 237–242