| Literature DB >> 16261636 |
Tímea Imre1, Gitta Schlosser, Gabriella Pocsfalvi, Rosa Siciliano, Eva Molnár-Szöllosi, Tibor Kremmer, Antonio Malorni, Károly Vékey.
Abstract
A new anionic surfactant (RapiGest SF) was successfully used for site-specific analysis of glycosylation in human alpha-1-acid glycoprotein (AGP). By means of this analytical approach combined with capillary HPLC-mass spectrometry (and tandem mass spectrometry), the N-linked glycosylation pattern of AGP was explored. On the basis of mass matching and MS/MS experiments ca 80 different AGP-derived glycopeptides were identified. Glycosylation shows a markedly different pattern for the various glycosylation sites. At sites I and II, triantennary complex-type oligosaccharides predominate and at sites III, IV and V, tetra-antennary complex-type oligosaccharides predominate. Sites IV and V show the presence of additional N-acetyl lactosamine (Gal-GlcNAc) units (even higher degree of branching and/or longer antennae are also present). Copyright 2005 John Wiley & Sons, LtdEntities:
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Year: 2005 PMID： 16261636 DOI： 10.1002/jms.938
Source DB: PubMed Journal: J Mass Spectrom ISSN： 1076-5174 Impact factor: 1.982