Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry of human alpha-1-acid glycoprotein
UNSPECIFIED. (2004) Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry of human alpha-1-acid glycoprotein. ANALYTICAL CHEMISTRY, 76 (17). pp. 4998-5005. ISSN 0003-2700Full text not available from this repository.
Official URL: http://dx.doi.org/10.1021/ac040019a
The ultrahigh resolution and sensitivity of electrospray ionization Fourier transform ion cyclotron resonance (ESI-FTICR) mass spectrometry have for the first time been exploited for the characterization of highly sialylated glycoproteins, using human alpha-1 -acid glycoprotein as the model compound. An alternative approach to the widely used high-performance liquid chromatography (HPLC) and matrix-assisted laser desorption/ionization (MALDI) assays is described. Ibis new method does not require any enzymatic or chemical digestion (removal of sialyl groups or deglycosylation), chemical derivatization (introduction of chromophore groups), or preliminary chromatographic separation (HPLC or electrophoresis). Following ESI and accumulation of ions in a hexapole ion guide, ions are injected into the ICR cell. A selected mass window from the overall ion population is isolated and axialized prior to detection. After acquisition and Fourier transform of the transient signal the resulted spectrum is evaluated in order to determine the charge state of the detected ions and the isotope pattern of the measured protein glycoform. The presence of ions from the same glycoform with different charge states was confirmed. The advantages and limitations of the technique are discussed. Future prospects and possible applications are indicated.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||ANALYTICAL CHEMISTRY|
|Publisher:||AMER CHEMICAL SOC|
|Official Date:||1 September 2004|
|Number of Pages:||8|
|Page Range:||pp. 4998-5005|
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