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Protein identification from 2‐DE gels by MALDI mass spectrometry
Author(s) -
Jungblut Peter,
Thiede Bernd
Publication year - 1997
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/(sici)1098-2787(1997)16:3<145::aid-mas2>3.0.co;2-h
Subject(s) - chemistry , mass spectrometry , chromatography , identification (biology) , matrix assisted laser desorption/ionization , organic chemistry , adsorption , desorption , botany , biology
Two‐dimensional electrophoresis (2‐DE) allows the separation of proteins at the level of protein species, which are defined by their chemical structure. Each chemical modification leads to a new protein species. Prerequisites for investigations of protein species are reproducible sample preparation, large gels (20 × 30 cm and larger), high sensitive detection methods, automated evaluation of gels, and sensitive methods for identification of 2‐DE‐separated protein species. MALDI mass spectrometry with its sensitivity in the fmol range fits with the sensitivity of protein detection on 2‐DE gels. Protein mass determination, peptide mass mapping, post‐source decay sequencing, and ladder sequencing by MALDI‐MS in combination with genome databases have the potential for complete structural investigation on the protein species level. The discrimination of 19 crystalline species of mouse eye lens and of 54 human heart heatshock protein 27 species shows the capacity of the combination of 2‐DE with MALDI‐MS. © 1997 John Wiley & Sons, Inc., Mass Spectrom Rev 16(3), 145–162, 1997