Abstract
It is difficult to isolate derivatives of α-crystallin with only one type of post-translational modification, because this protein is subjected to several different types of modification. In the present study using bovine lens proteins, we isolated mono-phosphorylated αB-crystallin with no other post-translational modifications. Using this material, we demonstrated that mono-phosphorylation reduced the activity of αB-crystallin by approximately 30%.Our results confirmed that investigation of the correlation between chaperone-like activities of α-crystallin and post-translational modification is important to understand the mechanism of cataract formation.
