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Abstract
The Raman spectra of a normal rabbit lens have been recorded over the range of 0 to 4000 cm-1. Spectral results indicate that protein conformation is predominantly beta-pleated sheet. Polarization measurements and assignments for most of the bands have been made; the spectral region for water indicates extensive hydrogen bonding. An N2 laser operating at 337 nm was used to produce cataracts in a rabbit lens; the Raman spectra of the cataractous lens were also recorded. Spectral changes are observable in the water region, and these are correlated with a mechanism of ultraviolet cataractogenesis.