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Updated: May 6, 2026

Matrix-assisted Laser Desorption/Ionization Time of Flight MALDI-TOF Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa
Published on: September 9, 2013
Peptide sequence determination by matrix-assisted laser desorption ionization employing a tandem double focusing
K F Medzihradszky1, G W Adams, A L Burlingame
1Department of Pharmaceutical Chemistry, Mass Spectrometry Facility, University of California, San Francisco, San Francisco, California, USA.
Abstract:
This report describes the fragmentation processes for peptides induced by collisional activation of the (12)C isobar of matrix-assisted laser desorption ionization (MALDI)-generated pseudomolecular ions employing an EBE orthogonal acceleration time-of-flight mass spectrometer and using xenon as the collision gas at a laboratory collision energy of 800 eV. These MALDI-collision-induced dissociation (CID) spectra are shown to provide sequence information of comparable quality to those obtained by using high energy CID conditions with liquid secondary ionization mass spectrometry on a four-sector tandem instrument. Peptide sequencing via MALDI-CID is demonstrated on three tryptic peptides obtained from a bacterial protein (P450 isozyme) of unknown sequence. Sensitivity is shown to be at the 1 pmol level for standard peptides.
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