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Mass spectrometric characterization of phosphorylated peptides using MALDI in‐source decay via redox reactions
Author(s) -
Asakawa Daiki,
Takayama Mitsuo
Publication year - 2012
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.2052
Subject(s) - chemistry , matrix assisted laser desorption/ionization , peptide , mass spectrometry , oxidizing agent , combinatorial chemistry , matrix (chemical analysis) , redox , molecule , small molecule , desorption , chromatography , biochemistry , organic chemistry , adsorption
Matrix‐assisted laser desorption/ionization in‐source decay (MALDI‐ISD) has been used for characterization of a phosphorylated peptides and proteins because labile phosphate group is not lost during the MALDI‐ISD process. The conventional MALDI‐ISD is initiated by the hydrogen transfer from reducing matrix molecules to peptide backbone, leading to c ′‐ and z ′‐series ions. In contrast, when an oxidizing chemical 5‐nitrosalicylic acid (5‐NSA) is served as the MALDI‐ISD matrix, a ‐ and x ‐series ions are specifically generated by hydrogen abstraction from peptide backbone to matrix molecule. The 5‐NSA provides useful complementary information to the conventional MALDI‐ISD for the analysis of amino acid sequencing and site localization of phosphorylation in peptides. The MALDI‐ISD with reducing and oxidizing matrix could be a useful method for the de novo peptide sequencing. Copyright © 2012 John Wiley & Sons, Ltd.