Abstract
gamma-secretase, the endoprotease which releases the C-terminus of beta A4 amyloid peptide, cleaves within the hydrophobic transmembrane domain of the amyloid precursor protein. In order to obtain a substrate for gamma-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).
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Alzheimer Disease / metabolism*
-
Amino Acid Sequence
-
Amyloid Precursor Protein Secretases
-
Amyloid beta-Peptides / chemistry
-
Amyloid beta-Peptides / genetics
-
Amyloid beta-Peptides / metabolism*
-
Aspartic Acid Endopeptidases
-
Binding Sites / genetics
-
Chromatography, High Pressure Liquid
-
Chromatography, Thin Layer
-
Endopeptidases / analysis*
-
Endopeptidases / metabolism*
-
Humans
-
Iodine Radioisotopes
-
Molecular Sequence Data
-
Peptide Fragments / chemical synthesis
-
Peptide Fragments / chemistry
-
Peptide Fragments / isolation & purification
-
Substrate Specificity
Substances
-
Amyloid beta-Peptides
-
Iodine Radioisotopes
-
Peptide Fragments
-
Amyloid Precursor Protein Secretases
-
Endopeptidases
-
Aspartic Acid Endopeptidases
-
BACE1 protein, human