Abstract
The soluble proteins of normal and cataractous lenses were separated according to their molecular size on the polysaccharide gel Sephadex G-100. In cataractous as well as in normal lenses 4 different components were obtained. During the evolution of eataract there is a preferential decrease of the low molecular weight proteins of the lens. These disappeared completely in mature and hypermature eataract. On the other hand, the proteins of high molecular weight (e.g., α-crystallin) are very resistant to the pathological process. The electrophoretic pattern of the low molecular weight proteins in the normal lens revealed several fractions distributed over a large mobility area. After immunoelectrophoresis, 3 different precipitin lines were obtained.
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