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Effect of sodium dodecyl sulfate micelles on peptide mass fingerprinting by matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Tummala Rama,
Limbach Patrick A.
Publication year - 2004
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.1588
Subject(s) - chemistry , sodium dodecyl sulfate , chromatography , mass spectrometry , peptide mass fingerprinting , matrix assisted laser desorption/ionization , peptide , trypsin , sample preparation in mass spectrometry , protein mass spectrometry , micelle , desorption , peptide sequence , bottom up proteomics , electrospray ionization , biochemistry , proteomics , organic chemistry , enzyme , aqueous solution , adsorption , gene
Here we have examined the effect of sodium dodecyl sulfate (SDS) at various concentrations on matrix‐assisted laser desorption/ionization (MALDI) peptide mass fingerprinting experiments. Several model proteins were digested with trypsin and then various amounts of SDS were added prior to MALDI mass spectrometry. Evaluation of the data was made by calculating the amino acid sequence coverage within each analysis. It was found that addition of 0.1–0.3% w/v SDS prior to MALDI analysis results in an increase in the number of tryptic peptides detected thereby improving the total sequence coverage of the analysis. The use of SDS at concentrations near its critical micelle concentration can improve sequence coverage from MALDI peptide mass fingerprinting analyses allowing for increased confidence in protein identification or additional opportunities to identify putative regions of posttranslational modification. Copyright © 2004 John Wiley & Sons, Ltd.