Abstract
1. Water-soluble crystallins from cortex and nucleus of both young and adult camel lenses were fractionated by gel filtration into high molecular weight aggregate (HMW-aggregate), alpha-low, beta-high, beta-low, gamma-high and gamma-low protein fractions. 2. Crystallins were characterized by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing (IEF). Changes related to age and lens parts were compared. 3. The major changes in crystallin distribution included an increase in HMW-aggregate (alpha-high), beta-high, and gamma, and a decrease in alpha-low and beta-low, when comparing lenses in the direction of the nucleus and in the direction of increasing age. 4. Similar changes were detected comparing either cortex and nucleus of the same lens or whole lenses of different age.