Serum protein profiling by solid phase extraction and mass spectrometry: a future diagnostics tool?
Serum protein profiling by MS is a promising method for early detection of disease. Important characteristics for serum protein profiling are preanalytical factors, analytical reproducibility and high throughput. Problems related to preanalytical factors can be overcome by using standardized and rigorous sample collection and sample handling protocols. The sensitivity of the MS analysis relies on the quality of the sample; consequently, the blood sample preparation step is crucial to obtain pure and concentrated samples and enrichment of the proteins and peptides of interest. This review focuses on the serum sample preparation step prior to protein profiling by MALDI MS analysis, with particular focus on various SPE methods. The application of SPE techniques with different chromatographic properties such as RP, ion exchange, or affinity binding to isolate specific subsets of molecules (subproteomes) is advantageous for increasing resolution and sensitivity in the subsequent MS analysis. In addition, several of the SPE sample preparation methods are simple and scalable and have proven easy to automate for higher reproducibility and throughput, which is important in a clinical proteomics setting.
Callesen
Anne K
AK
Protein Research Group, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark. anne.callesen@ouh.regionsyddanmark.dk
Madsen
Jonna S
JS
Vach
Werner
W
Kruse
Torben A
TA
Mogensen
Ole
O
Jensen
Ole N
ON
D000818:Animals; D001798:Blood Proteins / Q000032:analysis* / Q000737:chemistry; D002624:Chemistry, Clinical / Q000379:methods*; D006801:Humans; D013058:Mass Spectrometry; D052616:Solid Phase Extraction / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D001798:Blood Proteins