MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins.

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Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z ).

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MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins. MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins. The 28-kDa band from root PM enriched in hydrophobic proteins was digested by Lys-C. Phosphopeptides were enriched using a TiO2 column. All C-terminal phosphopeptides expected from root AtPIP aquaporins cannot be simultaneously recorded onto the same MS spectrum. The present spectrum illustrates the presence of the singly (m/z 1188.54) and diphosphorylated (m/z 1268.51) peptides of AtPIP2;1 and/or AtPIP2;2 (see text) and of the singly (m/z 1217.53) and diphosphorylated (m/z 1297.56) peptides of AtPIP2;7. *, metastable decomposition of peptide with m/z 1268.51. a.i., absolute intensity. Sodana Prak et al. Mol Cell Proteomics 2008;7:1019-1030 © 2008 The American Society for Biochemistry and Molecular Biology