Abstract
The presence of a non-dialyzable trypsin inhibitor has been demonstrated in lens extracts obtained from several different species. This trypsin inhibitor activity was found almost exclusively in the cortical region in both the bovine and the rabbit lens with little or no activity in either nucleus or capsule extracts. Agarose A-1·5 m gel filtration chromatography of rabbit lens soluble proteins showed one peak of trypsin inhibitor activity eluting at a molecular weight of about 50 000 daltons. Using the same technique, bovine lens extracts showed two peaks of trypsin inhibitor activity with molecular weights of about 3×10 5 daltons and 2×10 4 daltons. The presence of trypsin inhibitors in the cortical fiber cel's and their absence in the capsule epithelial cells of the bovine lens suggests that the differentiation of epithelial cells to fiber cells triggers the synthesis of these trypsin inhibitor proteins. Lens nuclear extracts, which did not contain active trypsin inhibitor, demonstrated trypsin-like proteolytic activity. This proteolytic activity was inhibited by the addition of lens extracts containing active trypsin inhibitor. These show that a binary system composed of a trypsin-like proteinase and an inhibitor exist in lens tissue.
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