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Improved matrix-assisted laser desorption/ionization mass spectrometric analysis of tryptic hydrolysates of proteins following guanidination of lysine-containing peptides.
- Source :
-
Rapid communications in mass spectrometry : RCM [Rapid Commun Mass Spectrom] 2000; Vol. 14 (21), pp. 2070-3. - Publication Year :
- 2000
-
Abstract
- Analysis of tryptic digests of proteins using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry commonly results in superior detection of arginine-containing peptides compared with lysine-containing counterparts. The effect is attributable in part to the greater stability of the arginine-containing peptide ions associated with the sequestration of the single ionizing proton on the arginine side-chain. Reaction of peptides with O-methylisourea resulted in conversion of lysine to homoarginine residues with consequent improved detection during MALDI-MS. Analysis of the underivatized tryptic digest of the yeast protein, enolase, revealed peptides representing 20% of the protein; the corresponding figure after derivatization was 46%.
- Subjects :
- Alcohol Dehydrogenase metabolism
Amino Acid Sequence
Fungal Proteins metabolism
Guanidines analysis
Methylurea Compounds metabolism
Molecular Sequence Data
Peptide Fragments chemistry
Phosphopyruvate Hydratase analysis
Phosphopyruvate Hydratase chemistry
Phosphopyruvate Hydratase metabolism
Trypsin metabolism
Yeasts
Guanidines metabolism
Homoarginine metabolism
Lysine metabolism
Peptide Fragments analysis
Peptide Fragments metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization methods
Subjects
Details
- Language :
- English
- ISSN :
- 0951-4198
- Volume :
- 14
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Rapid communications in mass spectrometry : RCM
- Publication Type :
- Academic Journal
- Accession number :
- 11085420
- Full Text :
- https://doi.org/10.1002/1097-0231(20001115)14:21<2070::AID-RCM133>3.0.CO;2-G