Riboflavin status and photo-induced riboflavin binding to the proteins of the rat ocular lens.

The presence of radioactivity in lenses of rats injected intraperitoneally with a solution of tryptophan and 14C-riboflavin, irradiated during 48 hours and under N2 atmosphere, was detected. The excitation fluorescence spectrum (lambda emission = 520 nm) of the soluble lens fraction corresponds to the riboflavin decomposition product of lumichrome type. When 14C-riboflavin enriched lenses were exposed to visible light, a photo-induced binding between riboflavin and a water insoluble protein fraction of the lenses was observed. This finding may help to clarify the lens modifications during aging and in cataractogenesis.