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Mass spectrometric identification of amino acid thiohydantoins
Author(s) -
Suzuki Tateo,
Song KyungDuck,
Itagaki Yasuhiro,
Tuzimura Katura
Publication year - 1976
Publication title -
organic mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0030-493X
DOI - 10.1002/oms.1210110602
Subject(s) - tripeptide , peptide , mass spectrometry , chemistry , protein mass spectrometry , peptide sequence , residue (chemistry) , cleavage (geology) , electron ionization , chromatography , peptide bond , stereochemistry , tandem mass spectrometry , biochemistry , ionization , organic chemistry , biology , paleontology , ion , fracture (geology) , gene
Amino acid thiohydantoins were identified using electron impact and chemical ionization mass spectrometry. Some fragmentations of thiohydantoin ring were also identified. These results suggest that the thiohydantoin method should be useful for the stepwise peptide sequence analysis starting from the carboxyl terminus. The sequence of a model tripeptide was determined by the combination of the thiohydantoin method and mass spectrometry. In the case of peptide which contained a proline residue as their C‐terminal peptide, cleavage of the peptide bond cannot be achieved.