Publikation:

Site Specific Identification of N-Linked Glycosylation in Proteins by Liquid Chromatography Electrospray Ionization Tandem Mass Spectrometry

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Springer_LifeSci_2008_Perdivara.pdf
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2008

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Perdivara, Irina
Iacob, Roxana Elena
Tomer, Kenneth B.

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POPESCU, Crisan, ed. and others. Applications of Mass Spectrometry in Life Safety. Dordrecht: Springer, 2008, pp. 109-120

Zusammenfassung

Recently, we reported the characterization of the glycans attached at the 11 N-glycosylation sites of Hepatitis C virus E2 envelope glycoprotein by tandem mass spectrometry. Infections caused by Hepatitis C virus represent the main cause of liver diseases such as hepatitis, cirrhosis and hepatocellular carcinoma. The N-linked sugars consist primarily of high mannose glycans, with structures ranging from the minimal core structure, Man3GlcNAc2 (Man3) up to 12 hexose residues attached to the GlcNAc-ß(l 4)-GlcNAc core (depicted as Hex3Man9GlcNAc2). Furthermore, the site N41 (N423) was observed to contain complex type glycans with the structures Man3-GlcNAc and Man3-GlcNAcFuc, in addition to the high mannose population Man3 through Man6, while the site N48 (N430) was occupied exclusively with complex type glycans (Man3-Fuc, Man3-GlcNAcFuc and Man3-GlcNAc2Fuc). The present contribution summarizes our experimental observations upon the factors which may have an impact on the CID tandem mass spectra of glycopeptides.

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ISO 690PERDIVARA, Irina, Roxana Elena IACOB, Michael PRZYBYLSKI, Kenneth B. TOMER, 2008. Site Specific Identification of N-Linked Glycosylation in Proteins by Liquid Chromatography Electrospray Ionization Tandem Mass Spectrometry. In: POPESCU, Crisan, ed. and others. Applications of Mass Spectrometry in Life Safety. Dordrecht: Springer, 2008, pp. 109-120
BibTex
@incollection{Perdivara2008Speci-9923,
  year={2008},
  title={Site Specific Identification of N-Linked Glycosylation in Proteins by Liquid Chromatography Electrospray Ionization Tandem Mass Spectrometry},
  publisher={Springer},
  address={Dordrecht},
  booktitle={Applications of Mass Spectrometry in Life Safety},
  pages={109--120},
  editor={Popescu, Crisan},
  author={Perdivara, Irina and Iacob, Roxana Elena and Przybylski, Michael and Tomer, Kenneth B.}
}
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    <dcterms:abstract xml:lang="eng">Recently, we reported the characterization of the glycans attached at the 11 N-glycosylation sites of Hepatitis C virus E2 envelope glycoprotein by tandem mass spectrometry. Infections caused by Hepatitis C virus represent the main cause of liver diseases such as hepatitis, cirrhosis and hepatocellular carcinoma. The N-linked sugars consist primarily of high mannose glycans, with structures ranging from the minimal core structure, Man3GlcNAc2 (Man3) up to 12 hexose residues attached to the GlcNAc-ß(l 4)-GlcNAc core (depicted as Hex3Man9GlcNAc2). Furthermore, the site N41 (N423) was observed to contain complex type glycans with the structures Man3-GlcNAc and Man3-GlcNAcFuc, in addition to the high mannose population Man3 through Man6, while the site N48 (N430) was occupied exclusively with complex type glycans (Man3-Fuc, Man3-GlcNAcFuc and Man3-GlcNAc2Fuc). The present contribution summarizes our experimental observations upon the factors which may have an impact on the CID tandem mass spectra of glycopeptides.</dcterms:abstract>
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