Characterization of the N-linked glycans of a murine monoclonal antibody 12A1 by LC/MS/MS

Fang Wang, Antonio Nakouzi, Ruth H. Angeletti, Arturo Casadevall

Research output: Contribution to conferencePaper

Abstract

The N-linked glycans of murine mAb 12A1 were characterized by LC/MS/MS coupled with Glu-C digestion in denature condition. The 12A1 were reduced and carboxyamidomethylated in 6 M GdHCl and 0.25 M phosphate buffer. Glu-C digestion was performed. The digestion was separated by micro HPLC and detected by the quadrupole ion trap mass spectrometer. The oligosaccharide chains of this antibody were characterized at N glycosylation site of Asn-363.

Original languageEnglish (US)
Pages469-470
Number of pages2
StatePublished - Dec 1 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
CountryUnited States
CityOrlando, FL
Period6/2/026/6/02

ASJC Scopus subject areas

  • Spectroscopy

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  • Cite this

    Wang, F., Nakouzi, A., Angeletti, R. H., & Casadevall, A. (2002). Characterization of the N-linked glycans of a murine monoclonal antibody 12A1 by LC/MS/MS. 469-470. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.