Resolving and assigning N-linked glycan structural isomers from ovalbumin by IMS-MS |
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Authors: | Manolo D Plasencia Dragan Isailovic Samuel I Merenbloom Yehia Mechref David E Clemmer |
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Institution: | Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA. |
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Abstract: | Ion mobility-mass spectrometry (IMS-MS) and molecular modeling techniques have been used to characterize ovalbumin N-linked
glycans. Some glycans from this glycoprotein exist as multiple isomeric forms. The gas-phase separation makes it possible
to resolve some isomers before MS analysis. Comparisons of experimental cross sections for selected glycan isomers with values
that are calculated for iterative structures generated by molecular modeling techniques allow the assignment of sharp features
to specific isomers. We focus here on an example glycan set, each having a m/z value of 1046.52 with formula H5N4+2Na]2+, where H corresponds to a hexose, and N to a N-acetylglucosamine. This glycan appears to exist as three different isomeric forms that are assignable based on comparisons
of measured and calculated cross sections. We estimate the relative ratios of the abundances of the three isomers to be in
the range of ∼1.0:1.35:0.85 to ∼1.0:1.5:0.80. In total, IMS-MS analysis of ovalbumin N-linked glycans provides evidence for
19 different glycan structures corresponding to high-mannose and hybrid type carbohydrates with a total of 42 distinct features
related to isomers and/or conformers. |
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