Our proposed research is to study the human lens low molecular weight proteins and to study how they are affected by aging and the cataractous processes. We will isolate and identify the low molecular weight human normal and cataractous lens proteins (i.e. Betas, GammaH, GammaL1 and GammaL2 crystallins) using gel filtration and a series of chromatofocusing. The purification of human lens low molecular weight protein is necessary before any possible relationship of these components to the classical crystallin groups can be clarified. These human lens low molecular weight proteins appear to be involved in the high molecular weight aggregates with conformational changes. The smallest of these proteins. GammaL2 crystallin possesses the unusual size of 11,000 dalton components and seems to be the break down product of other crystallins. We hope to identify the sauce of GammaL2 crystallin by immunochemical and chemical analyses. One process of studying the mechanism of aggregation is by ozonation. Ozonation of these low molecular weight proteins lead to the high molecular weight protein aggregates and small molecular weight fragments on gel filtration. Moreover, we plan to compare the aging effects of the absorption and fluorescence of the various types of human cataractous lens sections with those of the human normal lens section.