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.
Salim-Hanna
M
M
Pontificia Universidad Católica de Chile, Facultad de Química, Santiago.
Valenzuela
A
A
Silva
E
E
D000818:Animals; D003459:Crystallins / Q000378:metabolism*; D005260:Female; D007908:Lens, Crystalline / Q000378:metabolism* / Q000528:radiation effects; D008027:Light; D010084:Oxidation-Reduction; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains; D012256:Riboflavin / Q000378:metabolism*
D003459:Crystallins; D012256:Riboflavin