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A synthetic substrate assay for the gamma‐secretase of the β‐A4 amyloid of alzheimer's disease
Author(s) -
Evin Geneviève,
Beyreuther Konrad,
Masters Colin L.
Publication year - 1995
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.310010205
Subject(s) - chemistry , peptide , cleavage (geology) , amyloid precursor protein , agarose , senile plaques , amyloid precursor protein secretase , biochemistry , transmembrane protein , amyloid (mycology) , alzheimer's disease , biology , receptor , disease , medicine , inorganic chemistry , paleontology , pathology , fracture (geology)
γ‐secretase, the endoprotease which releases the C‐terminus of βA4 amyloid peptide, cleaves within the hydrophobic transmembrane domain of the amyloid precursor protein. In order to obtain a substrate for γ‐secretase, a dodecapeptide which spans the cleavage site was synthesized, labelled with 125‐iodine and conjugated to an agarose gel. A radiometric solid‐phase assay was developed using this immobilized substrate. Peptide products were separated by reverse‐phase HPLC and TLC to allow characterization of the cleavage site(s).