Abstract
Experiments with calf lens protein fractions in aqeous buffer solutions at room temperature showed that βH ‐ and βL ‐ and γ‐crystallin fractions became opaque following ultraviolet exposure at 308 nm, while the α‐crystallin fraction remained transparent. Transmission loss, due to UV‐irradiation, for all of the crystallin samples was studied in the concentration range of 0.1 mg/mL to 1.0 mg/mL, and for α‐ and γ‐crystallin, in the range up to 5 mg/mL. With increased concnetrations of βH‐,βL‐and γ‐crystallin, the rate of opacification increased. However, with α‐crystallin, the loss of transmission was negligble for all of the concentrations and irradiation times studied. Opacification of the crystallins was accompanied by formation of higher molecular weight insoluble proteins as detected by SDS‐PAGE.