2.7. Peptide analysis by MALDI-ToF MS

GL Grace M. Loxley
DH David O. Hooks
AA Aristotelis Antonopoulos
AD Anne Dell
SH Stuart M. Haslam
WL Wayne L. Linklater
JH Jane L. Hurst
RB Robert J. Beynon
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Peptides were analysed by MALDI-TOF mass spectrometry to acquire the masses of peptides derived from band-specific proteins. MALDI-TOF spectra were acquired using a Bruker ultrafleXtreme mass spectrometer in reflectron mode. Samples were mixed with MALDI matrix (saturated solution of α-cyano-4-hydroxycinnamic acid in 50% (v/v) ACN/0.2% (v/v) TFA) in a 1 : 1 ratio and spotted onto a target plate before being left to air dry. The laser frequency was 1000 Hz, laser energy 30% of maximum and 2000 laser shots were collected per spectrum, between 700–4000 m/z. All aspects of data acquisition and machine management were controlled through the flexControl, and data processing was performed in flexAnalysis (Bruker Daltonics).

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