Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry.

M. Belghazi (1) , K. Bathany (1) , Codjo Hountondji (2) , X. Grandier-Vazeille (3) , S. Manon (3) , J.-M. Schmitter (4)

1 IECB - Imagerie Moléculaire et Nanobiotechnologies - Institut Européen de Chimie et Biologie
2 BIOC - Laboratoire de Biochimie de l'Ecole polytechnique
3 IGBMC - Institut de Génétique et de Biologie Moléculaire et Cellulaire
4 LPTC - Laboratoire de Physico -& Toxico Chimie des systèmes naturels

In the context of proteome analysis, matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) can fulfil the two tasks of primary structure verification and protein identification. As an illustration of the first of these tasks, the sequence of Eschericha coli isoleucyl-tRNA synthetase, a protein with 15 reported sequence conflicts, has been established by means of MALDI mass mapping. The identification of mitochondrial proteins participating in a yeast supramolecular complex exhibiting NADH dehydrogenase activity highlights the performances of MALDI-MS for the second task. The spectral suppression phenomenon occurring for complex peptide mixtures analysed by MALDI is discussed, as well as the role of post-source decay analysis for confident protein identification.

Domains: Biochemistry, Molecular Biology

M. Belghazi, K. Bathany, Codjo Hountondji, X. Grandier-Vazeille, S. Manon, et al.. Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry.. Proteomics, 2001, 1 (8), pp.946-54. ⟨10.1002/1615-9861(200108)1:8<946::AID-PROT946>3.0.CO;2-P⟩. ⟨hal-00771534⟩