3. Mass spectrometry.
The development of mass spectrometry (MS) facilities within our laboratory, and for our institute and the university, has been an enormous asset. Since the acquisition of an electrospray mass spectrometer in 1997, the application of mass spectrometry techniques to protein identification, identification of sites of covalent modification and quantification of changes in protein expression has led to well over 30 joint publications. In our own research, it enabled us to identify new phosphorylation sites in the AMPK complex and to demonstrate that in heart, insulin antagonized AMPK activation during ischaemia via the PKB-induced phosphorylation of the α-subunits at Ser495/491.
2D-LC-LTQ ESI MS set-up
We are currently studying differential protein expression by label-free multidimensional LC-MS with a Thermo Finnigan LTQ ESI mass spectrometer equipped with ETD fragmentation. One application is the screening of glycoproteins from sera and cerebro-spinal fluid of patients with neurodegenerative diseases to discover biomarkers. We are also developing techniques for phosphoproteomics by hydrophilic interaction liquid chromatography (HILIC) followed by phosphopeptide enrichment on titanium oxide beads and analysis by on-line capillary LC-MS.
To know more... (pdf chapter of the last de Duve Institute report)
Publications >
