Glycosylation site analysis of human alpha-1-acid glycoprotein (AGP) by capillary liquid chromatography-electrospray mass spectrometry |
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Authors: | Imre Tímea Schlosser Gitta Pocsfalvi Gabriella Siciliano Rosa Molnár-Szöllosi Eva Kremmer Tibor Malorni Antonio Vékey Károly |
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Affiliation: | Department of Mass Spectrometry, Institute of Structural Chemistry, Chemical Research Center, Hungarian Academy of Sciences, 1525 Budapest, Hungary. |
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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). |
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Keywords: | alpha‐1‐acid glycoprotein RapiGest SF glycosylation glycopeptide mass spectrometry |
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