Charge derivatization by 4-sulfophenyl isothiocyanate enhances peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

• Published in: Journal of mass spectrometry. Vol. 38; no. 4; pp. 373 - 377
• Main Authors: Marekov, Lyuben N., Steinert, Peter M.
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.04.2003; Wiley
• Subjects: Amino Acid Sequence; Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Benzenesulfonates - chemistry; Biological and medical sciences; Calcium-Binding Proteins - chemistry; Calcium-Binding Proteins - metabolism; charge derivatization; Fundamental and applied biological sciences. Psychology; Humans; Isothiocyanates - chemistry; matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; Molecular Sequence Data; Peptide Fragments - chemistry; peptides; post-source decay; Proteins; Sequence Analysis, Protein; sequencing; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Transglutaminases - chemistry; Transglutaminases - metabolism; Trypsin - metabolism; charge derivatization; peptides; Matrix assisted laser desorption ionization; Derivatization; Sulfonic acid; Protein; Binding protein; Time of flight method; Organic isothiocyanate; matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; post-source decay; Mass spectrometry; Sequencing; Calmodulin; Structural analysis

High‐sensitivity, rapid identification of proteins in proteomic studies normally uses a combination of one‐ or two‐dimensional electrophoresis together with mass spectrometry. The simplicity and sensitivity of matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOFMS)...