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Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry analysis of proteins in human cerebrospinal fluid
Author(s) -
Westman A.,
Nilsson C. L.,
Ekman R.
Publication year - 1998
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19980831)12:16<1092::aid-rcm286>3.0.co;2-n
Subject(s) - chemistry , mass spectrometry , chromatography , mass spectrum , surface enhanced laser desorption/ionization , matrix assisted laser desorption/ionization , protein mass spectrometry , desorption , ionization , analytical chemistry (journal) , matrix (chemical analysis) , sample preparation in mass spectrometry , tandem mass spectrometry , electrospray ionization , ion , adsorption , organic chemistry
Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectra of proteins in cerebrospinal fluid analyzed without prior purification are presented. Less than 100 fmol amounts of proteins in the 10 000 to 20 000 u mass range and linked to human disease (multiple sclerosis, Alzheimer’s disease, and stroke) were detected in a complex mixture of proteins and peptides, in the presence of high concentrations of salts, lipids and free amino acids. The mass resolution was sufficient to distinguish between the non‐hydroxylated and hydroxylated forms of a 13 400 u protein. Simple fractionation of the cerebrospinal fluid using microbore‐reversed phase high performance liquid chromatography improved signal‐to‐noise ratios in the mass spectra. High‐accuracy peptide mass mapping and database searching were utilized to confirm the identity of several proteins. The presented results show that matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry could be used as a tool to perform rapid screening of chemically altered proteins in small volumes of biological fluids. © 1998 John Wiley & Sons, Ltd.