Abstract
Agar gel electrophoretic study on soluble human lens proteins revealed six major fractions with a maximum of 10 subfractions in normal lens. Similar number of major fractions was found in cataractous lenses, although there was progressive diminution of separation into subfractions. These fractions were grouped as the major proteins of the crystalline lens, i.e. α-, β- and γ-crystallins. No significant change in crystallin concentration could be observed in immature senile cataracts. Fall in γ-crystallin and rise in α-crystallin were statistically significant in advanced scuile cataracts of both nuclear and cortical varieties. In hypermature senile cataract fall in β-crystallin was also significant. In developmental cataract rise in α-crystallin and fall in β-crystallin were significant, while apparent fall in γ-crystallin was not significant statistically.
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