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- W2368085389 abstract "Identification of the glycated sites in proteins plays an important role in the field of protein glycation. In the present study, we have established a CID neutral-loss-triggered MS 3 method to analyze the glycated sites in proteins. ESI-CID-MS was used to stimulate multi-site cleavage in glycated Amadori peptides. MS 3 scans triggered by neutral losses of 3H 2 O and 3H 2 O + HCHO produced similar results in terms of glycated peptide identification. However, neutral loss of 3H 2 O resulted in more accurate glycated peptide identification in multi-stage activation experiments. The results showed that the K227 was more easily glycated by D-glucose when compared with the K229 in ovalbumin under dry heating conditions. Overall, the multi-stage activation approach could identify the glycation site in peptides with one glycosylation site." @default.
- W2368085389 created "2016-06-24" @default.
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- W2368085389 date "2013-01-01" @default.
- W2368085389 modified "2023-09-26" @default.
- W2368085389 title "Analysis of Glycated Peptides by Neutral-loss-triggered CID MS~3 Spectrometry" @default.
- W2368085389 hasPublicationYear "2013" @default.
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