Purpose: To evaluate the character of alpha-crystallin molecular chaperone activity in selenite cataract.
Methods: alpha-Crystallin from lenses of normal young rats and lenses with selenite cataract were separated and purified by gel filtration chromatography. The chaperone activity of alpha-crystallin was assayed by mearsuring heat-induced aggregation and scattering of catalase.
Results: alpha-Crystallin in both normal and cataractous lenses specifically prevented catalase against thermal aggregation compared with control proteins. The preventive ability in alpha H-crystallin was less than in alpha L-crystallin. Chaperone activity was diminished in selenite cataract. There was statistically significant difference in chaperone activity between normal and cataractous lenses in both alpha H-crystallin and alpha L-crystallin respectively.
Conclusion: The reduction of alpha-crystallin chaperone activity in selenite cataract by preventing thermal aggregation of catalase is an important process in cataract formation.