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. 2006 Mar;17(3):1261–1272. doi: 10.1091/mbc.E05-10-0927

Figure 5.

Figure 5.

Identification of phospho-tyrosine residues on the N-cadherin cytoplasmic domain after in vitro phosphorylation by Src. The spectra are shown in pairs showing peptides that had been subjected to the phosphorylation reaction either in the presence or the absence of ATP. Phosphorylated peptides occurred as new peaks with an extra 80 Da in mass. (A) The His-tagged N-cadherin cytoplasmic domain was phosphorylated in vitro by Src and then subjected to MALDI-TOF mass spectrometry analysis. (B and C) His-tagged N-cadherin cytoplasmic domain was phosphorylated in vitro by Src and then digested by trypsin. The tryptic peptides were subjected to MALDI mass spectrometry analysis. (B) Identification of the phosphorylated Y852, Y860, Y884, and Y886 residues in the peptide AADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPR (5448 Da). (C) Identification of phospho-Y820 in peptides MDERPIHAEPQYPVR (1838 Da) and RMDERPIHAEPQYPVR (1994 Da).