Abstract：
:Pathogenic events in Alzheimer's disease are believed to involve an imbalance between the production and clearance of the neurotoxic 42 amino acid form of the beta-amyloid peptide (Abeta1-42). Although much is known about the production of Abeta1-42, many questions remain about its degradation. Here, we describe an optimized automated immunoprecipitation mass spectrometry method that enables accurate and rapid monitoring of the major Abeta isoforms in cerebrospinal fluid. Furthermore, we describe a technique of antibody immobilization, minimizing background signals. The identities of these Abeta products were confirmed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and nanoflow liquid chromatography and tandem mass spectrometry with a hybrid linear trap Fourier transform ion cyclotron resonance mass spectrometer. Finally, we report the finding of two novel Abeta peptides (Abeta2-17 and Abeta3-17).
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Portelius E,Tran AJ,Andreasson U,Persson R,Brinkmalm G,Zetterberg H,Blennow K,Westman-Brinkmalm Adoi
10.1021/pr0703627subject
Has Abstractpub_date
2007-11-01 00:00:00pages
4433-9issue
11eissn
1535-3893issn
1535-3907journal_volume
6pub_type
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