BETA-SECRETASE ISOLATED FROM HUMAN 293 CELLS

摘要

Compositions comprising a protease isolated from human 293 cells or polypeptide fragments having about 85 % sequence homology with said protease are disclosed. The native protease is designated beta -secretase and cleaves beta -amyloid precursor protein on the amino-terminal side of the beta -amyloid peptide. The beta -secretase has an apparent MW from about 260-300 kD, when glycosylated and binds wheat germ agglutinin. A screening assay for identification of beta -secretase inhibitors shows that said beta -secretase is not inhibited by common inhibitors of serine, cysteine, aspartyl and metalloproteases.