HUMAN LENS ENZYME ALTERATIONS WITH AGE AND CATARACT - GLYCERALDEHYDE-3-P DEHYDROGENASE AND TRIOSE PHOSPHATE ISOMERASE

The isoelectric point distribution of G-3-P DH and TPI from human lenses was examined as a function of age and cataract formation. Both enzymes exhibited progressive heterogeneity with age and a shift towards an acidic charge. Little qualitative differences in the pI profiles of G-3-P DH and TPI were found to distinguish mixed cataracts from age comparable normal lenses. While the most alkaline form of G-3-P DH required less HAsO4-2 for optimal activity, no other kinetic property, i.e. Km substrate, cofactor and inhibitors distinguished any of the charge forms of G-3-P DH. All meta- or isozyme forms of TPI had the same Km substrate in the forward and reverse reaction direction. The most acidic forms of G-3-P DH and TPI were less stable to increased temperatures than their more alkaline counterparts suggesting a decreased stability.