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

Imre, Timea and Schlosser, Gitta (Vácziné) and Pocsfalvi, G. and Siciliano, R. and Molnár-Szöllősi, É. and Kremmer, Tibor and Vékey, Károly (2005) Glycosylation site analysis of human alpha-1-acid glycoprotein (AGP) by capillary liquid chromatography-electrospray mass spectrometry. JOURNAL OF MASS SPECTROMETRY, 40 (11). pp. 1472-1483. ISSN 1076-5174

Text 1214726.pdf Restricted to Repository staff only Download (997kB) | Request a copy

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 AGPderived 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).

Actions (login required)

Edit Item