Photosensitized acceleration of riboflavin on the formation of lenticular HMW-protein aggregation
Ono, S.; Hirano, H.
International Journal for Vitamin and Nutrition Research. Internationale Zeitschrift für Vitamin- und Ernahrungsforschung. Journal International de Vitaminologie et de Nutrition 57(4): 401-403
1987
ISSN/ISBN: 0300-9831 PMID: 3440715 Document Number: 304861
The percentage of high molecular weight protein aggregates obtained by Sepharose 6B column chromatography was increased significantly at pH 9.0 as compared to that of at pH 4.0 and 7.0, especially by exposure to light. The authors suggest that aggregation of lens protein is induced by light-exposure in the presence of riboflavin at higher pH's and that riboflavin acts as a photosensitizer to form high molecular weight protein aggregates in the lens.