A comparison of aerobic and anerobic photolysis of lens protein

Abstract

The soluble protein fraction from the cortex of calf lens (ca. 2·5 mg/ml in phosphate buffer, pH 7·4) was photolyzed under both aerobic and anerobic environments. The photolyzed protein was kept at ambinet temperatures, and filters were employed to exclude light Upon photolysis, human lens protein from 14- and 72-year-old normal lenses undergo a photodestruction similar to that found in calf lens protein. But old human lens protein does not give a similar increase of non-tryptophan fluorescence, suggesting that a pre-existing modification prevented its formation.