Endogeneous peptide profiling of cerebrospinal fluid by MALDI-TOF mass spectrometry

Autor: Thang V. Pham, Laura F. van der Voort, Charlotte E. Teunissen, Connie R. Jimenez, Marleen J. A. Koel-Simmelink
Přispěvatelé: Internal medicine, Laboratory Medicine, Amsterdam Neuroscience - Neurodegeneration
Jazyk: angličtina
Rok vydání: 2007
Předmět:
Zdroj: Jimenez, C R, Koel-Simmelink, M, Pham, T V, van der Voort, L & Teunissen, C E 2007, ' Endogeneous peptide profiling of cerebrospinal fluid by MALDI-TOF mass spectrometry : Optimization of magnetic bead-based peptide capture and analysis of preanalytical variables ', Proteomics-Clinical Applications, vol. 1, no. 11, pp. 1385-1392 . https://doi.org/10.1002/prca.200700330
Proteomics-Clinical Applications, 1(11), 1385-1392. Wiley-VCH Verlag
ISSN: 1862-8346
Popis: Cerebrospinal fluid (CSF) perfuses the brain and spinal cord. CSF contains peptides and proteins important for brain physiology and potentially also relevant to brain pathology. High-throughput endogeneous peptide profiling by MS is an emerging approach for disease diagnosis and biomarker discovery. A magnetic bead-based method for off-line serum peptide capture coupled to MALDI-TOF-MS has been introduced recently. In this study, we optimize the peptide capture method for profiling of CSF and investigate the effect of a number of preanalytical variables. The CSF profiles contain ∼100 reliably detected peptides at m/z 800-4000 with reproducible ion intensities (average 7% CV). The investigated preanalytical variables include: time at room temperature (RT) before storage, storage temperature, freeze-thawing cycles, and blood contamination. The CSF peptidome (
Databáze: OpenAIRE
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