Further studies on elastase-like activity in normal and cataractous lenses

Abstract

Ca++ was not found to be essential for the activation of the latent elastase in normal lenses. However, the activities increased 70–100% in human, bovine, sheep and goat lenses at a concentration of 5.0×10−3M of CaCl2. On the other hand, in cataractous human lenses, Ca++ inhibited the process of activation. The activation process however, seems to be a divalent metal ion dependent process since ethylene diamine tetra acetate (2.0×10−3M) blocked the activation of the elastase-like enzyme in both normal and cataractous lenses. p-Hydroxy mercuribenzoate (10−4M) and benzamidine (1.65×10−2M) also blocked the activation process, indicating that a trypsin-like enzyme requiring sulfhydryl groups, is involved in the activation of latent elastase.