Summary
Novelty: The purification of human amyloidin protease, the generation of antibodies specific for the enzyme, and the isolation and in vitro expression of its cognate gene, are reported.
Biology: Methods for the purification of amyloidin protease from human tissue are provided. The enzyme has an appparent molecular weight of 80 kDa and proteolytically cleaves a Met-Asp peptide bond in the amyloid precursor protein which releases the mature Asp terminus of the β-amyloid peptide. An assay for inhibitors of the protease is described, and antibodies raised against the enzyme are provided. The isolation and characterization of the cognate gene is described together with methods for expressing the recombinant protein in vitro. Inhibitors of the enzyme may have use for the therapeutic intervention of Alzheimer's disease, and antibodies raised against it may have diagnostic use.