Human cathepsin F: expression in baculovirus system, characterization and inhibition by protein inhibitors

Recombinant full-length human procathepsin F, produced in the baculovirus expression system, was partially processed during the purification procedure to a form lacking the N-terminal cystatin-like domain and activated with pepsin. Active cathepsin F efficiently hydrolyzed Z-FR-MCA (k/K=106 mM[-1]s[-1]) and Bz FVR-MCA (k/K=8 mM[-1]s[-1]), whereas hydrolysis of Z-RR- MCA was very slow (k/K