Glycosylation site analysis of human alpha-1-acid glycoprotein (AGP) by capillary liquid chromatography—electrospray mass spectrometry

✍ Scribed by Tímea Imre; Gitta Schlosser; Gabriella Pocsfalvi; Rosa Siciliano; Éva Molnár-Szöllősi; Tibor Kremmer; Antonio Malorni; Károly Vékey

• Book ID: 102904183
• Publisher: John Wiley and Sons
• Year: 2005
• Tongue: English
• Weight: 974 KB
• Volume: 40
• Category: Article
• ISSN: 1076-5174
• DOI: 10.1002/jms.938

✦ Synopsis

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, Ltd.