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Characterization of Protein Oligosaccharides Using MSn

sup> on a fragment which has already undergone these losses in a previous stage of MS (Figure 3b, m/z 1333.7), cross-ring fragment products emerge, revealing the nature of saccharide linkages in the molecule. Similar results can be achieved for N5H5-II by MSn of the ion at m/z 1606.8 from MS2.


Figure 3a-b. MS3 and MS4 for isolation and characterization of glycan N5H5-I.

The oligosaccharide in Figure 1b is a heavily GlcNAcylated oligosaccharide of ovalbumin. The MS2 spectrum of the doubly-sodiated ion (Figure 4) is dominated by ions corresponding to the loss of non-reducing terminal GlcNAc sugars. No other information is obtainable due to the sup-pression of other bond cleavages. By reducing the collision energies to 35 units and using MS3-6, one can not only count terminal GlcNAc residues in a facile manner, but can produce a species upon MS7 which is no longer susceptible to suppression effects (Figure 5). MS8 of this ion subsequently reveals the locations of the previously attached GlcNAc residues, indicating three acetylaminosugars on one mannose antenna, a fourth and fifth on the other arm, and a sixth residing on the bisected mannose of the core (Figure 6).


Figure 4. MS2 of the ovalbumin glycan GlcNAc8Man3.

The use of higher collision energies to remove two or three residues per stage of MSn can also produce the m/z 1087.8 ion in fewer steps. These alternate MSn experiments yield the same structural information by MS5 or MS6, suggesting that perhaps the structura
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