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. 2012 Jun 25;287(33):27851–27862. doi: 10.1074/jbc.M112.376525

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 5. — Electrospray mass spectrometry of intact lateral flagellin protein from Aeromonas hydrophila AH-3. a, electrospray mass spectrum of intact lateral flagellin protein, showing an envelope of multiply charged protein ions. b, the reconstructed molecular mass profile of lateral flagellin, showing masses at 29,703, 30,424, 30,819, and 30,899 Da. This corresponds in total to three sites of modification with a 376-Da glycan moiety. c, tandem mass spectrometry analysis of the multiply charged protein ion at m/z 1186. A peptide type y ion fragmentation series was observed, the sequence of which corresponded to the C-terminal peptide of the lateral flagellin LSNSNQMTGMVTGLLR. In addition, several ions were observed that did not correspond to peptide fragment ions, observed at m/z 377, with likely daughter ion at 359 due to loss of water. , 376-Da sugar.

Inline graphic — Electrospray mass spectrometry of intact lateral flagellin protein from Aeromonas hydrophila AH-3. a, electrospray mass spectrum of intact lateral flagellin protein, showing an envelope of multiply charged protein ions. b, the reconstructed molecular mass profile of lateral flagellin, showing masses at 29,703, 30,424, 30,819, and 30,899 Da. This corresponds in total to three sites of modification with a 376-Da glycan moiety. c, tandem mass spectrometry analysis of the multiply charged protein ion at m/z 1186. A peptide type y ion fragmentation series was observed, the sequence of which corresponded to the C-terminal peptide of the lateral flagellin LSNSNQMTGMVTGLLR. In addition, several ions were observed that did not correspond to peptide fragment ions, observed at m/z 377, with likely daughter ion at 359 due to loss of water. , 376-Da sugar.