Abstract
In the aging and cataractous human lens, soluble protein decreases and insoluble protein increases in concentration. This change is more marked in the cataractous than in the aging normal lens. Of the soluble lens proteins, γ-crystallin decreases and α-crystallin increases in both aging and cataract formation, and this change is more pronounced in the cataract. In the human, as in bovine lenses, α-crystallin and albuminoid appear to be more closely related than any of the other fractions. Senile normal lenses and senile cataracts resemble each other as seen in their amino acid analyses, E11 values and sulfhydryl content. In the human lens, albuminoid appears to derive from α-crystalling mostly (as in bovine lens), not from γ-erystallin as in the rat and dogfish.
Published Version
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