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MALDI‐MS for C‐terminal sequence determination of peptides and proteins degraded by carboxypeptidase Y and P
Author(s) -
Thiede Bernd,
Wittmann-Liebold Brigitte,
Bienert Michael,
Krause Eberhard
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01323-s
Subject(s) - exopeptidase , chemistry , carboxypeptidase , peptide , mass spectrometry , matrix assisted laser desorption/ionization , trypsin , carboxypeptidase a , biochemistry , peptide sequence , chromatography , amino acid , myoglobin , protein mass spectrometry , enzyme , tandem mass spectrometry , desorption , organic chemistry , adsorption , gene
Matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) has been used for C‐terminal amino acid sequence determination of peptides and proteins. The usefulness of MALDI‐MS was demonstrated by analyzing peptide mixtures (C‐terminal peptide ladder) which were generated by enzymatic digestion of substance P, glucagon, angiotensinogen, insulin B chain and myoglobin with the exopeptidases carboxypeptidase Y and P. The results clearly show that up to 11 amino acid residues can be determined in the pmol range by analyzing the molecular masses of the truncated peptides. For proteins it is possible to investigate enzymatic or chemical digests in the same manner.