Aspirin prevents the nonenzymatic glycosylation and carbamylation of the human eye lens crystallins in vitro. 
When the human eye lens homogenate which was incubated with [14C]-acetylsalicylic acid (aspirin) and separated into alpha-, beta-, and gamma - crystallins by Sepharose 6B gel-filtration, the radiolabel was found in all the three crystallins.  The significant decreases in the free zeta-amino groups of aspirin treated crystallins as compared to the untreated ones indicate the probable sites of acetylation in the crystallins.  The inhibition of the binding of [14C]-glucose and [14C]-cyanate to the aspirin pre-treated crystallins suggests that prior acetylation with aspirin prevents the occurrence of the nonenzymatic glycosylation and carbamylation of the lens crystallins in vitro.