Quantitative analysis of amyloid- peptides in cerebrospinal fluid using immunoprecipitation and MALDI-Tof mass spectrometry
| Autor: | John E. Hale, David M. Holtzman, Robert A. Dean, Valentina Gelfanova, Martin R. Farlow, Deborah I. Fisher, Richard E. Higgs, Karen Cox, Eric Siemers, Zhaoyan Jin, Yue Wei Qian, Xiaohua He, Amechand Boodhoo |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Gene isoform
Amyloid beta-Peptides Chromatography Immunoprecipitation Coefficient of variation Enzyme-Linked Immunosorbent Assay Biology MALDI-TOF Mass Spectrometry Mass spectrometry Biochemistry Peptide Fragments Amyloid β peptide Cerebrospinal fluid Alzheimer Disease Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization mental disorders Genetics Humans Protein Isoforms Molecular Biology Quantitative analysis (chemistry) Biomarkers |
| Zdroj: | Briefings in Functional Genomics and Proteomics. 6:149-158 |
| ISSN: | 1477-4062 1473-9550 |
| Popis: | Immunoprecipitation (IP) combined with matrix-assisted laser desorption ionization (MALDI) time of flight (Tof) mass spectrometry has been used to develop quantitative assays for amyloid-beta (Abeta) peptides in cerebrospinal fluid (CSF). Inclusion of (15)N labelled standard peptides allows for absolute quantification of multiple Abeta isoforms in individual samples. Characterization of variability associated with all steps of the assay indicated that the IP step is the single largest contributor to overall variability. Optimization of the assay resulted in overall coefficient of variation |
| Databáze: | OpenAIRE |
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