title: Changes of lens crystallins photosensitized with tryptophan metabolites.
abstract: The effect of UV irradiation on bovine lens soluble proteins (crystallins) in the presence of tryptophan metabolites was investigated in vitro. The cross-linking of crystallins by UV irradiation was accelerated by kynurenine, 3-hydroxykynurenine, anthranilic acid and 3-hydroxyanthranilic acid. On denaturation of crystallins by photooxidation, alpha-crystallin was characterized by the formation of water-soluble HMW (high molecular weight) protein, while water-insoluble HMW protein was produced from beta- and gamma-crystallin. These HMW aggregates showed cross-linking by non-disulfide covalent bonds. LMW (low molecular weight) peptides were formed by degradation of alpha- and beta-crystallin.
authors: Department of Biophysical Chemistry, Faculty of Pharmaceutical Sciences, Meijo University, Nagoya, Japan.
authors: H
authors: H
authors: Ichijima
authors: S
authors: S
authors: Iwata
mesh_terms: D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003459:Crystallins / Q000378:metabolism*; D007908:Lens, Crystalline / Q000378:metabolism*; D011838:Radiation-Sensitizing Agents / Q000494:pharmacology*; D012995:Solubility; D014364:Tryptophan / Q000378:metabolism*; D014466:Ultraviolet Rays
chemical_list: D003459:Crystallins; D011838:Radiation-Sensitizing Agents; D014364:Tryptophan