March 1982
Volume 22, Issue 3
Articles  |   March 1982
Crosslinking and photoreaction of ozone-oxidized calf-lens alpha-crystallin.
Investigative Ophthalmology & Visual Science March 1982, Vol.22, 402-405. doi:
  • Views
  • PDF
  • Share
  • Tools
    • Alerts
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      E Fujimori; Crosslinking and photoreaction of ozone-oxidized calf-lens alpha-crystallin.. Invest. Ophthalmol. Vis. Sci. 1982;22(3):402-405. doi:

      Download citation file:

      © ARVO (1962-2015); The Authors (2016-present)

  • Supplements
This content is PDF only. Please click on the PDF icon to access.

Direct-photo-oxidation, singlet oxygen-oxidation, or photosensitized oxidation can modify lens crystallins, causing an increase in blue fluorescence and covalent crosslinking. A relationship between these changes has not been elucidated. We now report results from experiments with ozone oxidation. When calf-lens alpha-crystallin is treated with zone oxidation. When calf-lens alpha-crystallin is treated with ozone, new absorption, fluorescence, and phosphorescence, which are characteristic of the oxidized product of tryptophan (N-formylkynurenine), appear at 320, 435, and 445 nm, respectively. In addition, in this ozonization of alpha-crystallin, its polypeptides are crosslinked by nondisulfide bonds. Irradiation of ozone-treated alpha-crystallin with near-ultraviolet (365 nm) light increases crosslinking and reduces the 320 nm absorbance with a concomitant appearance of a new absorption at about 420 nm. This photoproduct exhibits an intense fluorescence around 450 nm and a weak phosphorescence at 510 nm, with excitation peaks at 400, 415, and 422 nm. These findings are essentially the same as those observed in photo-oxidized alpha-crystallin, suggesting the involvement of the same tryptophan oxidized product in the modification of the lens protein.


This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.