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Effect of residual acrylamide monomer from two‐dimensional gels on matrix‐assisted laser desorption/ionization peptide mass mapping experiments
Author(s) -
Alvarez Erwin J.,
Larsen Barbara S.,
Coldren Christopher D.,
Rice Janet
Publication year - 2000
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/(sici)1097-0231(20000615)14:11<974::aid-rcm974>3.0.co;2-h
Subject(s) - chemistry , acrylamide , monomer , desorption , matrix assisted laser desorption/ionization , matrix (chemical analysis) , pipette , ionization , chromatography , peptide , residual , mass spectrometry , signal (programming language) , analytical chemistry (journal) , polymer , adsorption , organic chemistry , biochemistry , ion , algorithm , computer science , programming language
Residual acrylamide can cause severe suppression of signal intensity during matrix‐assisted laser desorption/ionization (MALDI) peptide mass mapping experiments. This suppression phenomenon can compromise the ability to detect low picomole and subpicomolar amounts of peptides extracted from two‐dimensional gels. A rapid and simple method that exploits the use of pipette tips incorporating C18 packing materials for the enhancement of MALDI signal intensity is presented. The utility of the method is demonstrated with peptide solutions incorporating residual acrylamide and/or gel monomer components. Copyright © 2000 John Wiley & Sons, Ltd.