Specificity of Rat Liver Cathepsin D

Abstract

The specificity of highly purified rat liver cathepsin D was investigated by analyzing the digests of denatured proteins. At the P1 site, cathepsin D prefers hydrophobic residues except Ile and Val, that are branched at the β-carbon. Strong and weak hydrophobicities are required at P1' and P2 sites, respectively. A lower protency for β-turn formation is essential for the sequence around the P1 site.