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Detection and quantitation of cellularly derived amyloid β peptides by immunoprecipitation‐HPLC‐MS
Author(s) -
Clarke Nigel J,
Tomlinson Andy J,
Ohyagi Yasumasa,
Younkin Steven,
Naylor Stephen
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00706-6
Subject(s) - immunoprecipitation , peptide , chemistry , mass spectrometry , amyloid precursor protein , amyloid (mycology) , chromatography , high performance liquid chromatography , alzheimer's disease , amyloid β , microbiology and biotechnology , biochemistry , biology , disease , medicine , gene , inorganic chemistry
A quantitative method for detection of amyloid β peptides using immunoprecipitation‐HPLC‐mass spectrometry (IP‐LC‐MS) is described. Comparison of IP‐LC‐MS with sandwich ELISA revealed comparable results in the analysis of Aβ 1–40 and Aβ 1–42 derived from fetal guinea pig cell media and cell lysates. The use of IP‐LC‐MS not only allows a quantitative method for Aβ 1–40 and Aβ 1–42 peptides present in Alzheimer's disease (AD), but allows detection of other Aβ peptide species that may also play a role in the onset of AD in humans.