Abstract
Blue-fluorescent α-crystallin and a blue-fluorescent low molecular weight species have been isolated from calf lenses by gel-filtration on Sephadex G-200. This α-crystallin with considerable light-scattering has a single fluorescence maximum at 420 nm. The blue fluorescence of the α-crystallin is enhanced in the presence of p-mercuribenzoate, which is capable of partially dissociating the aggregated protein. The comparison of blue-fluorescent α-crystallin isolated from cow, calf and embryonic lenses shows an age-related increase of blue fluorescence. Blue-fluorescent water-insoluble proteins also increase with age.
Keywords:
Bovine lens,
Lens proteins,
α-Crystallin,
Aggregation,
Fluorescence,
Aging,
Sulfhydryl modification
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© 1978 S. Karger AG, Basel
1978
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