Asparaginyl endopeptidase mapping of proteins with subsequent matrix-assisted laser desorption/ionization mass spectrometry
Article first published online: 8 APR 2005
Copyright © 1995 John Wiley & Sons, Ltd.
Rapid Communications in Mass Spectrometry
Volume 9, Issue 12, pages 1095–1100, 1995
How to Cite
Kanda, F., Yoshida, S., Okumura, T. and Takamatsu, T. (1995), Asparaginyl endopeptidase mapping of proteins with subsequent matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom., 9: 1095–1100. doi: 10.1002/rcm.1290091203
- Issue published online: 8 APR 2005
- Article first published online: 8 APR 2005
- Manuscript Accepted: 23 AUG 1995
- Manuscript Received: 8 AUG 1995
A matrix-assisted laser desorption/ionization (MALDI) mass spectrometric mapping strategy for the identification and characterization of isolated and purified proteins is described. The method, which employs the combined usage of a new site-specific enzyme Asparaginyl endopeptidase (Asn-EP) for proteolysis, and MALDI for subsequent mass analysis, is capable of rapidly and sensitively examining the components of complex mixtures without any chromatographic or electrophoretic separation steps. Subpicomole sample quantities typically suffice to permit the confirmation of deduced primary structures and/or the identification of possible post-translational modifications. The data obtained should also prove useful for mass matching and sequence homology searching of computerised protein sequence data bases of known proteins.