http://www.cnr.it/ontology/cnr/individuo/prodotto/ID45638
Glycosylation site analysis of human alpha-1-acid glycoprotein (AGP) by capillary liquid chromatography electrospray mass spectrometry (Articolo in rivista)
- Type
- Label
- Glycosylation site analysis of human alpha-1-acid glycoprotein (AGP) by capillary liquid chromatography electrospray mass spectrometry (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/jms.938 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Imre T.; Schlosser G.; Pocsfalvi G.; Siciliano R.; Moln-Szllosi E.; Kremmer T.; Malorni A.; Vekey K. (literal)
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- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Department of Mass Spectrometry, Institute of Structural Chemistry, Chemical Research Center, Hungarian Academy of Sciences, 1525 Budapest,
Hungary;
Research Group of Peptide Chemistry, Hungarian Academy of Sciences, Eotvos L. University, Budapest 112, Hungary;
Instituto di Scienze dell' Alimentazione, Consiglio Nazionale Delle Ricerche, Avellino, Via Roma 52 a-c. 83100, Italy;
Department of Biochemistry, National Institute of Oncology, H-1122 Budapest, Hungary (literal)
- Titolo
- Glycosylation site analysis of human alpha-1-acid glycoprotein (AGP) by capillary liquid chromatography electrospray mass spectrometry (literal)
- 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 (literal)
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