Age-dependent deamidation of alpha B-crystallin

Abstract

Bovine and human alpha B-crystallin undergo deamidation upon aging in the lens. In bovine alpha B-crystallin, the specific site of deamidation has been identified by peptide mapping after tryptic digestion. Asn-146 was found to be subject to deamidation, whereas the only other asparagine residue, at position 78, is not affected. Asn-146 is flanked at the carboxylic side by a glycyl residue. Yet, the rate of in vivo deamidation is low. In vitro studies reveal that the deamidation is accompanied by significant racemization, indicating that the deamidation proceeds via formation of a succinimide intermediate.