title: Riboflavin status and photo-induced riboflavin binding to the proteins of the rat ocular lens.
abstract: 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.
authors.affiliation: Pontificia Universidad Católica de Chile, Facultad de Química, Santiago.
authors.forename: M
authors.initials: M
authors.lastname: Salim-Hanna
authors.forename: A
authors.initials: A
authors.lastname: Valenzuela
authors.forename: E
authors.initials: E
authors.lastname: Silva
mesh_terms: 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*
chemical_list: D003459:Crystallins; D012256:Riboflavin