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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2005

Contributo in rivista

Tipo: Articolo in rivista

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

Anno di pubblicazione: 2005

Formato: Elettronico

Autori: Imre T.; Schlosser G.; Pocsfalvi G.; Siciliano R.; Moln-Szllosi E.; Kremmer T.; Malorni A.; Vekey K.

Affiliazioni autori: 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

Autori CNR:

  • ANTONIO MALORNI
  • GABRIELLA KATALIN POCSFALVI
  • ROSA ANNA SICILIANO

Lingua: inglese

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

Lingua abstract: inglese

Pagine da: 1472

Pagine a: 1483

Rivista:

Journal of mass spectrometry Wiley,
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 1076-5174

Numero volume: 40

Numero fascicolo: 11

DOI: 10.1002/jms.938

Referee: Sė: Internazionale

Indicizzato da: ISI Web of Science (WOS) [000233482400008]

Parole chiave:

  • alpha-1-acid glycoprotein
  • RapiGest SF
  • glycosylation
  • glycopeptide
  • mass spectrometry

Strutture CNR:

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