Modification of calf lens crystallins as determined by gel electrophoresis.
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.
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
D003459:Crystallins; D013451:Sulfonic Acids; D014508:Urea