Combination of two matrices results in improved performance of MALDI MS for peptide mass mapping and protein analysis.
A new sample preparation method for MALDI based on the use of a mixture of the two commonly used matrices, DHB and CHCA, is described. The matrix mixture preparation results in increased sequence coverage and spot-to-spot reproducibility for peptide mass mapping compared to the use of the single matrix components. This results in more reliable protein identification in proteomics studies and facilitates automated data acquisition. This method shows better tolerance towards salts and impurities, eliminating the need for pre-purification of the samples. It has also been found to be advantageous for the analysis of intact proteins, and especially for glycoproteins. The mixture allows the presence of rather high concentrations of urea in the sample solutions.
Laugesen
Sabrina
S
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Roepstorff
Peter
P
D006023:Glycoproteins / Q000032:analysis / Q000737:chemistry; D010449:Peptide Mapping / Q000379:methods*; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000032:analysis* / Q000737:chemistry; D020543:Proteome / Q000032:analysis / Q000737:chemistry; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D014357:Trypsin
D006023:Glycoproteins; D010455:Peptides; D011506:Proteins; D020543:Proteome; D014357:Trypsin