Photosensitized acceleration of riboflavin on the formation of lenticular HMW-protein aggregation.
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.
Department of Biochemistry, School of Medicine, Iwate Medical University, Morioka, Japan.
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D000818:Animals; D002845:Chromatography; D003459:Crystallins / Q000378:metabolism* / Q000528:radiation effects; D006863:Hydrogen-Ion Concentration; D008027:Light; D046911:Macromolecular Substances; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D012256:Riboflavin / Q000494:pharmacology*
D003459:Crystallins; D046911:Macromolecular Substances; D012256:Riboflavin