Further studies on elastase-like activity in normal and cataractous lenses |
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| Authors: | S Swaminathan T N Pattabiraman |
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| Institution: | 1. Department of Biochemistry, Kasturba Medical College, 576 119, Manipal, India
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| 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. |
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