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J Chromatogr A. 2007 Jul 13;1156(1-2):183-7. Epub 2007 Apr 22.

Characterization of a novel modification on IgG2 light chain. Evidence for the presence of O-linked mannosylation.

Author information

1
Analytical Sciences, Amgen Inc., 1201 Amgen Court West, Seattle, WA 98119, USA. martinet@amgen.com

Abstract

This paper describes the analysis of a novel modification identified on the light chain of a recombinant IgG2 antibody. This modification, a +162 Da adduct, suggestive of a single hexose addition, was observed by mass analysis of the reduced molecule. The modification was located on residue serine 66 of the light chain by investigation with LC-MS peptide mapping, mass spectrometry and N-terminal sequencing techniques. Location of the adduct on serine pointed the investigation toward O-linked glycosylation. Identification of the hexose residue was deduced from its elimination by action of alpha-mannosidase, providing evidence for the presence of an O-mannosylated light chain. This type of modification in the glycosylation profile of antibodies, to our knowledge, has not been reported for human IgG molecules.

PMID:
17493628
DOI:
10.1016/j.chroma.2007.04.050
[Indexed for MEDLINE]

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