Acidic lens-protein degrading activity in bovine ciliary body. III. Lens crystallin degradation by fractions A and B.
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.
D000143:Acids / Q000378:metabolism; D000818:Animals; D002417:Cattle; D005591:Chemical Fractionation; D002845:Chromatography; D002924:Ciliary Body / Q000378:metabolism*; D003459:Crystallins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration
D000143:Acids; D003459:Crystallins