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

Item Type:	Article
Title:	MALDI-MS for C-terminal sequence determination of peptides and proteins degraded by carboxypeptidase Y and P
Creators Name:	Thiede, B. and Wittmann-Liebold, B. and Bienert, M. and Krause, E.
Abstract:	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.
Keywords:	MALDI-MS, C-Terminal Sequencing, Carboxypeptidase, Animals, Horses, Swine
Source:	FEBS Letters
ISSN:	0014-5793
Publisher:	Elsevier
Volume:	357
Number:	2
Page Range:	65-69
Date:	2 January 1995
Official Publication:	https://doi.org/10.1016/0014-5793(94)01323-S
PubMed:	View item in PubMed

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