To investigate the effects of UV-B exposure on the protein solutions of different lens parts, rabbit lenses were separated into the equator (Eq), anterior cortex (Ac), nucleus (Nu) and posterior cortex (Pc). After homogenization, the water-soluble protein from each part was irradiated with UV-B at 0 to 0.225 J/cm<sup>2</sup>. Alterations in the content of protein SH, carbonyl groups, light scattering intensity and SDS-PAGE pattern were measured to compare the effect of UV-B on the protein solutions of various lens parts with or without additional GSH to test its preventive effect. The results showed that after UV-B irradiation, the protein sulfhydryl groups are gradually reduced. The nonprotein thiol (GSH added to the protein solution) was lost more rapidly than the protein sulfhydryl. The high molecular bands on the SDS-PAGE pattern mainly aggregated with disulfide. UV-B damage also increased the content of carbonyl groups and light scattering, irrespective of the lens parts. Lens proteins from the equator suffered the least damage while those of the nucleus were most strongly affected by UV-B exposure. This study suggests that the lens proteins from various lens parts have different responses to UV-B exposure; the sensitivity was in the following order: Eq < Ac ≤ Pc < Nu.