Improved matrix-assisted laser desorption/ionization mass spectrometric analysis of tryptic hydrolysates of proteins following guanidination of lysine-containing peptides.
作者： Francesco L. Brancia , Stephen G. Oliver , Simon J. Gaskell
DOI: 10.1002/1097-0231(20001115)14:21<2070::AID-RCM133>3.0.CO;2-G
关键词:
摘要: Analysis of tryptic digests proteins using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry commonly results in superior detection arginine-containing peptides compared with lysine-containing counterparts. The effect is attributable part to the greater stability peptide ions associated sequestration single ionizing proton on arginine side-chain. Reaction O-methylisourea resulted conversion lysine homoarginine residues consequent improved during MALDI-MS. underivatized digest yeast protein, enolase, revealed representing 20% protein; corresponding figure after derivatization was 46%.
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