MALDI-MS for C-terminal sequence determination of peptides and proteins degraded by carboxypeptidase Y and P.
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.
Thiede
B
B
Max-Delbrück-Zentrum für Molekulare Medizin, Abt. Proteinchemie, Berlin-Buch, Germany.
Wittmann-Liebold
B
B
Bienert
M
M
Krause
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases / Q000378:metabolism*; D006736:Horses; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017421:Sequence Analysis / Q000379:methods*; D013552:Swine
D010446:Peptide Fragments; C025427:carboxypeptidase P; D002268:Carboxypeptidases; C022633:serine carboxypeptidase