Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry of Human -1-Acid Glycoprotein
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文摘
The ultrahigh resolution and sensitivity of electrosprayionization Fourier transform ion cyclotron resonance(ESI-FTICR) mass spectrometry have for the first timebeen exploited for the characterization of highly sialylatedglycoproteins, using human lpha.gif" BORDER=0>-1-acid glycoprotein as themodel compound. An alternative approach to the widelyused high-performance liquid chromatography (HPLC)and matrix-assisted laser desorption/ionization (MALDI)assays is described. This new method does not requireany enzymatic or chemical digestion (removal of sialylgroups or deglycosylation), chemical derivatization (introduction of chromophore groups), or preliminary chromatographic separation (HPLC or electrophoresis). Following ESI and accumulation of ions in a hexapole ionguide, ions are injected into the ICR cell. A selected masswindow from the overall ion population is isolated andaxialized prior to detection. After acquisition and Fouriertransform of the transient signal the resulted spectrumis evaluated in order to determine the charge state of thedetected ions and the isotope pattern of the measuredprotein glycoform. The presence of ions from the sameglycoform with different charge states was confirmed. Theadvantages and limitations of the technique are discussed.Future prospects and possible applications are indicated.

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