- Original Article
- Open Access
Assessment of protein stability in cerebrospinal fluid using surface-enhanced laser desorption/ionization time-of-flight mass spectrometry protein profiling
Clinical Proteomics volume 2, pages 91–101 (2006)
Recent studies have evaluated proper acquisition and storage procedures for the use of serum or plasma for mass spectrometry (MS)-based proteomics. The present study examines the proteome stability of human cerebrospinal fluid (CSF) over time at 23°C (room temperature) and 4°C using surface-enhanced laser desorption/ionization time-of-flight MS. Data analysis revealed that statistically significant differences in protein profiles are apparent within 4 h at 23°C and between 6 and 8 h at 4°C. Inclusion of protease and phosphatase inhibitor cocktails into the CSF samples failed to significantly reduce proteome alterations over time. We conclude that MS-based proteomic analysis of CSF requires careful assessment of sample collection procedures for rapid and optimal sample acquisition and storage.
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Ranganathan, S., Polshyna, A., Nicholl, G. et al. Assessment of protein stability in cerebrospinal fluid using surface-enhanced laser desorption/ionization time-of-flight mass spectrometry protein profiling. Clin Proteom 2, 91–101 (2006). https://doi.org/10.1385/CP:2:1:91
- Phosphatase Inhibitor
- Relative Peak Intensity
- Proteomic Alteration
- Surface Enhance Laser Desorption Ionization
- Sample Collection Procedure