|
|
||||||||
Investigative Ophthalmology & Visual Science, Vol 27, 98-102, Copyright © 1986 by Association for Research in Vision and Ophthalmology
ARTICLES AND REPORTS |
GN Rao and E Cotlier
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.
This article has been cited by other articles:
![]() |
P. Saxena, A. K. Saxena, X.-L. Cui, M. Obrenovich, K. Gudipaty, and V. M. Monnier Transition Metal-Catalyzed Oxidation of Ascorbate in Human Cataract Extracts: Possible Role of Advanced Glycation End Products Invest. Ophthalmol. Vis. Sci., May 1, 2000; 41(6): 1473 - 1481. [Abstract] [Full Text] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |