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Characterization of Protein Oligosaccharides Using MSn

solution to these problems encountered with MS/MS. The removal of monosaccharide and disaccharide substituents by successive stages of MSn not only provides a facile method for obtaining sequence information, but can produce ion species which themselves yield fragments of greater variety and higher relative intensity. As a result, the LCQ Series reveals structural details otherwise lost by traditional tandem MS, and provides a new approach to the mass spectrometric characterization of protein glycans.2

Goal

To demonstrate:
How MSn can be used in oligosaccharide analysis to determine monosaccharide sequence and composition, carbohydrate branching, and monosaccharide linkages.
The ability of MSn to perform separate characterizations of two isobaric oligosaccharides, even when infused into the LCQ Series as an unseparated mixture.
That early stages of MSn can remove labile substituents, producing an ion substrate which yields previously unattainable information when subjected to further stages of MSn.


Figure 1a. Two HexNAc5Hex5 glycans released from chicken ovalbumin.
Figure 1b. GlcNAc8Man3 oligosaccharide from chicken ovalbumin.

Experimental Conditions


Oligosaccharides were released from hen ovalbumin by hydrazinolysis and were used as an unseparated mixture. The oligosaccharides were then dissolved in a slurry of sodium hydroxide and dimethyl sulfoxide, permethylated with methyl iodide, and extracted into chloroform per Ciucanu and Kerek.3

LCQ Conditions


Ionization method: ESI
Sample introduction: direct infusion, 3-5 L/min
with LCQ syrin
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Source:


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