Distribution and some properties of cathepsin B in the bovine eyes

Cathepsin B in the bovine eye was studied biochemically using α- N-benzoyl- l-arginine amide as substrate. The highest specific activity of cathepsin B was observed in the ciliary body among bovine eye tissues, the activity being highest in the lysosomal fraction. The optimal pH of the enzyme in the ciliary body was about 5·1. The enzyme activity in the ciliary body was activated by thiol agents, and inhibited by p-chloromercuribenzoate, leupeptin and heavy metal ions.