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Characterization of Protein Oligosaccharides Using MSn

ge pump
Sample conditions: 50 ng/L total mixture in
50:50 MeOH/water, 1 mM sodium acetate
Capillary temperature: 200C
Needle voltage: +4.5-5 kV
Sheath gas: nitrogen, 30 unit
Collision energies: 60-65 units, except where noted


Figure 2. MS2 of m/z 1169.5, the doubly-sodiated molecular ion of N5H5-I and N5H5-II.

Results

Figure 1a shows two oligosaccharides from the ovalbumin carbohydrate mixture. Since galactose and mannose are both hexoses, and therefore diastereomers of one another, both permethylated oligosaccharides have the same composition (HexNAc5Hex5) and molecular weight (2293 Da). With these two oligosaccharides infused together, MS2 of their doubly-sodiated molecular ions at m/z 1169.5 (Figure 2) produces fragments corresponding to both N5H5-I and N5H5-II, with each oligosaccharide effectively contaminating the spectrum of the other.

The fragment at m/z 937.7 corresponds to loss of a Hex-HexNAc disaccharide antenna, which is a structural feature only found on N5H5-I. Therefore, selecting the m/z 937.7 ion and subjecting it to MS3 (Figure 3a) yields structural information on N55H5-I, even as N5H55-II is continuously infused into the instrument. Favorable cleavage sites lie adjacent to GlcNAc residues, particularly terminal GlcNAcs, resulting in the preferred fragmentation of glycosidic bonds (noted by B and Y labels) and suppression of cross-ring fragments (A and X-type ions).4 By performing MSn'"/>

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