title: Modification of calf lens crystallins as determined by gel electrophoresis.
abstract: Variations in size and charge of calf lens proteins, particularly gamma crystallins, were studied by polyacrylamide gel electrophoresis. Exposure of gamma crystallins to near-UV light in the presence of L-tryptophan produces species of higher electrophoretic mobility and higher retardation. Treatment with urea and sulfonation also produced changes in the retardation co-efficient. The increase of retardation co-efficient of gamma crystallin is interpreted to be a result of conformational changes. Gamma crystallins are particularly sensitive to photo-modification, and this process may be associated with age-related changes in the lens.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003459:Crystallins / Q000528:radiation effects; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008433:Mathematics; D008970:Molecular Weight; D011485:Protein Binding; D013451:Sulfonic Acids; D014466:Ultraviolet Rays; D014508:Urea
chemical_list: D003459:Crystallins; D013451:Sulfonic Acids; D014508:Urea