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. 2003 Oct 23;17(22):2528–2534. doi: 10.1002/rcm.1236

Figure 1.

Figure 1

MALDI‐MS and μ‐HPLC/MALDI‐MS measurements on N‐terminal Gln, carboxyamidomethyl‐Cys, and their −17 Da products. (a, b) Spectra of two consecutive LC fractions containing glycosylated fragments from human integrin beta1 (477–490) CHEG[N]GTFECGACR (fraction 16) and its cyclization product (fraction 17); (c) MALDI‐MS spectra of in‐gel digested SARS virus nucleocapsid protein (1163–1190 Da range); (d, e) spectra of fractions 19 and 21, containing unmodified QYNVTQAFGR peptide and its pyroGlu‐ analog, respectively; (f) MALDI‐MS spectra showing degradation of the CEVFR (6–10) fragment from bovine α‐lactalbumin (1 mg/mL digest); (g, h) μ‐HPLC fractionation of the same peptides (2 pmol injected) from the 17‐protein digest mixture. Note that it was not possible even to examine the latter fragments before chromatographic separation of the 17‐protein digest, because of poor S/N ratios. See experimental for conditions.