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Identification of proteins separated by one‐dimensional sodium dodecyl sulfate/polyacrylamide gel electrophoresis with matrix‐assisted laser desorption/ionization ion trap mass spectrometry; comparison with matrix‐assisted laser desorption/ionization time‐of‐flight mass fingerprinting
Author(s) -
Zeng Rong,
Chen YongBing,
Shao XiaoXia,
Shieh ChiaHui Paul,
Miller Ken,
Tran Helen,
Xia QiChang
Publication year - 2003
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1143
Subject(s) - chemistry , mass spectrometry , matrix assisted laser desorption/ionization , chromatography , ionization , desorption , surface enhanced laser desorption/ionization , protein mass spectrometry , analytical chemistry (journal) , peptide mass fingerprinting , time of flight mass spectrometry , sodium dodecyl sulfate , matrix (chemical analysis) , ion trap , gel electrophoresis , sample preparation in mass spectrometry , ion , proteomics , tandem mass spectrometry , electrospray ionization , biochemistry , adsorption , organic chemistry , gene
Digests from ten gel bands containing low abundance proteins were analyzed by both matrix‐assisted laser desorption/ionization ion trap (MALDI‐IT) and matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐TOF) mass spectrometry (MS) methods. MALDI‐TOF techniques were able to identify only one protein from all 10 gel bands, while MALDI‐IT identified eight proteins from the same 10 bands. The ability to perform MS/MS experiments with a MALDI‐IT instrument leads to protein identifications based on both peptide molecular mass and sequence information, and is much less prone to errors and uncertainties introduced by peptide fingerprinting methodologies in which protein identification is based on peptide molecular masses alone. Copyright © 2003 John Wiley & Sons, Ltd.