The u
ltrahigh reso
lution and sensitivity of e
lectrosprayionization Fourier transform ion cyc
lotron resonance(ESI-FTICR) mass spectrometry have for the first timebeen exp
loited for the characterization of high
ly sia
ly
latedg
lycoproteins, using human
![](/images/gifchars/a<font color=)
lpha.gif" BORDER=0>-1-acid g
lycoprotein as themode
l compound. An a
lternative approach to the wide
lyused high-performance
liquid chromatography (HPLC)and matrix-assisted
laser desorption/ionization (MALDI)assays is described. This new method does not requireany enzymatic or chemica
l digestion (remova
l of sia
ly
lgroups or deg
lycosy
lation), chemica
l derivatization (introduction of chromophore groups), or pre
liminary chromatographic separation (HPLC or e
lectrophoresis). Fo
llowing ESI and accumu
lation of ions in a hexapo
le ionguide, ions are injected into the ICR ce
ll. A se
lected masswindow from the overa
ll ion popu
lation is iso
lated andaxia
lized prior to detection. After acquisition and Fouriertransform of the transient signa
l the resu
lted spectrumis eva
luated in order to determine the charge state of thedetected ions and the isotope pattern of the measuredprotein g
lycoform. The presence of ions from the sameg
lycoform with different charge states was confirmed. Theadvantages and
limitations of the technique are discussed.Future prospects and possib
le app
lications are indicated.