PMID: 3761742Jan 1, 1986Paper

Acidic lens-protein degrading activity in bovine ciliary body. III. Lens crystallin degradation by fractions A and B

Japanese Journal of Ophthalmology
S HayasakaI Kabasawa

Abstract

We studied the in vitro digestion of lens crystallin by two fractions (Fractions A and B) of acidic lens-protein degrading activity from the bovine ciliary body. With whole lens crystallin as substrate, Fraction A degraded beta L-crystallin most significantly, and beta H-, gamma-, and alpha-crystallins moderately. Fraction B degraded alpha-crystallin most significantly, beta H- and beta L-crystallins moderately, and gamma-crystallin slightly. Insoluble protein was most resistant to digestion by Fractions A and B. Crystallins from the lens cortex and nucleus were degraded in the same manner as those from the whole lens.

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