MALDI‐MS for C‐terminal sequence determination of peptides and proteins degraded by carboxypeptidase Y and P

FEBS Letters

Krause, Eberhard¹  Thiede, Bernd²  Bienert, Michael¹  Wittmann-Liebold, Brigitte² 

[1] Forschungsinstitut für Molekulare Pharmakologie, Alfred-Kowalke-Str. 4, D-10315 Berlin, Germany;Max-Delbrück-Zentrum für Molekulare Medizin, Abt. Proteinchemie, D-13125 Berlin-Buch, Germany

关键词: MALDI-MS;    C-Terminal sequencing;    Carboxypeptidase;    MALDI-MS;    matrix assisted laser desorption/ionization mass spectrometry;    LC-MS;    liquid chromatography mass spectrometry;    CPY;    carboxypeptidase Y;    CPP;    carboxypeptidase P;    TFA;    trifluoroacetic acid;    Da;    Dalton;   

DOI  :  10.1016/0014-5793(94)01323-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown