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Abstract
The free epsilon-amino groups and 5-hydroxymethylfurfural (5-HMF) contents were determined in soluble and insoluble proteins of clear human lenses and diabetic and nondiabetic senile cataractous lenses. The free epsilon-amino group content of soluble proteins in diabetic cataracts was decreased by 37% (P less than 0.01), whereas in nondiabetic senile cataracts it did not differ from that of clear lenses. The free epsilon-amino group content of insoluble proteins both in diabetic and nondiabetic cataracts was decreased significantly (P less than 0.001, P less than 0.015, respectively). The 5-HMF content of soluble proteins in diabetic cataracts was increased by 52% (P less than 0.001), whereas in nondiabetic cataracts it did not change from that of clear lenses. The 5-HMF content of insoluble proteins in diabetic as well as in nondiabetic cataracts was increased significantly as compared to that of clear lens (P less than 0.001, P less than 0.001, respectively). The soluble protein of diabetic and nondiabetic cataracts was decreased with an increase in the insoluble protein content. These results suggest that nonenzymatic glycosylation plays a role in the conformational change of lens proteins in both diabetic and nondiabetic cataracts.