Identification of photooxidation sites in bovine alpha-crystallin.

  title={Identification of photooxidation sites in bovine alpha-crystallin.},
  author={E L Finley and Mark Busman and James W. Dillon and Rosalie K. Crouch and Kevin L. Schey},
  journal={Photochemistry and photobiology},
  volume={66 5},
Because UV irradiation of proteins can produce reactive oxygen species and exposure to UV light has been implicated in cataractogenesis, the sites of photooxidation of bovine alpha-crystallin, a major lens protein with molecular chaperone activity, were identified using tandem mass spectrometry (MS/MS). Bovine alpha-crystallin was irradiated with UV light (> 293 nm) for 1, 4 and 8 h, digested with trypsin and analyzed by matrix-assisted laser desorption ionization, time-of-flight mass… CONTINUE READING


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