Protein identification in cerebrospinal fluid using packed capillary liquid chromatography Fourier transform ion cyclotron resonance mass spectrometry.
The identification and characterization of proteins in complex biological samples such as body fluids, require powerful and reliable tools. Mass spectrometry is today one of the most important methods in such research. This paper reports on the results from the first experiment where a tryptic digest of cerebrospinal fluid was analyzed applying reversed phase liquid chromatography coupled on-line to a 9.4 T Fourier transform ion cyclotron resonance mass spectrometer. In total, 70 204 peaks were detected, which originated from 16 296 isotopic clusters corresponding to 6551 unique peptide masses. From these masses, 39 proteins were identified in the sample. The amount of sample required for one experiment corresponds to 32 microL of cerebrospinal fluid.
Ramström
Margareta
M
Institute of Chemistry, Department of Analytical Chemistry, Uppsala University, Uppsala, Sweden.
Palmblad
Magnus
M
Markides
Karin E
KE
Håkansson
Per
P
Bergquist
Jonas
J
D001703:Biophysics / Q000379:methods; D002555:Cerebrospinal Fluid / Q000378:metabolism*; D002853:Chromatography, Liquid / Q000379:methods*; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D010455:Peptides / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D014357:Trypsin / Q000494:pharmacology
D010455:Peptides; D014357:Trypsin