EFFECT OF GALACTOSE ON ALPHA-CRYSTALLIN

Chromatographic separation of alpha-crystallin incubated with [H-3]-la belled galactose showed the radioactivity to be concentrated in the lo w molecular mass subunits (20 and 40 kDa). The effect of glycation on the structural organization of alpha-crystallin was evaluated by FPLC analysis of native (pH 6.8 and 8.2) and glycated protein in dissociati ng conditions. Results suggest that the glycation acts on the protein surface by altering its charge distribution.