Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry

Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry

Tryptic digests of three proteins are reacted with O‐methylisourea in order to convert lysine residues to homoarginines. The resulting homoarginine‐terminated peptides exhibit more intense MALDI mass spectral peaks than their lysine‐terminated predecessors. This simple chemical reaction should there...

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Veröffentlicht in:Rapid communications in mass spectrometry 2000-12, Vol.14 (23), p.2147-2153
Hauptverfasser: Beardsley, Richard L., Karty, Jonathan A., Reilly, James P.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Animals
Cattle
Databases, Factual
Guanine - chemistry
Hemoglobins - chemistry
Hemoglobins - metabolism
Humans
Lysine - chemistry
Methylurea Compounds - chemistry
Molecular Sequence Data
Peptide Mapping - methods
Peptides - analysis
Peptides - chemistry
Serum Albumin, Bovine - chemistry
Serum Albumin, Bovine - metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
Trypsin - chemistry
Trypsin - metabolism
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Zusammenfassung:Tryptic digests of three proteins are reacted with O‐methylisourea in order to convert lysine residues to homoarginines. The resulting homoarginine‐terminated peptides exhibit more intense MALDI mass spectral peaks than their lysine‐terminated predecessors. This simple chemical reaction should therefore facilitate protein sequencing and mass mapping. Copyright © 2000 John Wiley & Sons, Ltd.
ISSN:0951-4198
1097-0231
DOI:10.1002/1097-0231(20001215)14:23<2147::AID-RCM145>3.0.CO;2-M