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Clinical Chemistry 0: clinchem.2004.047308v1, 2005; 10.1373/clinchem.2004.047308
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Received on December 23, 2004
Accepted on April 4, 2005

Proteomics and Protein Markers

Standardized Approach to Proteome Profiling of Human Serum Based on Magnetic Bead Separation and Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry

Sven Baumann 1, Uta Ceglarek 1, Georg Martin Fiedler 2, Jan Lembcke 2, Alexander Leichtle 2, Joachim Thiery 2*

1 Institute of Laboratory Medicine, Clinical Chemistry and Molecular Diagnostics, University Hospital, Leipzig, Germany, and These authors contributed equally to this work
2 Institute of Laboratory Medicine, Clinical Chemistry and Molecular Diagnostics, University Hospital, Leipzig, Germany

* To whom correspondence should be addressed. E-mail: thiery{at}medizin.uni-leipzig.de.

Background: Magnetic bead purification for the analysis of low-abundance proteins in body fluids facilitates the identification of potential new biomarkers with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The aim of our study was to establish a proteome fractionation technique and to validate a standardized blood sampling, processing, and storage procedure for proteomic pattern analysis.

Methods: We used magnetic bead separation for proteome profiling of human blood by MALDI-TOF MS (mass range, 1000-10 000 Da) and studied the effects on the quality and reproducibility of the proteome analysis of anticoagulants, blood clotting, time and temperature of sample storage, and the number of freeze-thaw cycles of samples.

Results: The proteome pattern of human serum was characterized by ~350 signals in the mass range of 1000-10 000 Da. The proteome profile showed time-dependent dynamic changes before and after centrifugation of the blood samples. Serum mass patterns differed between native samples and samples frozen once. The best reproducibility of proteomic patterns was with a single thawing of frozen serum samples.

Conclusion: Application of the standardized preanalytical blood sampling and storage procedure in combination with magnetic bead-based fractionation decreases variability of proteome patterns in human serum assessed by MALDI-TOF MS.


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