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Age‐dependent deamidation of αB‐crystallin
Author(s) -
Groenen Patricia J.T.A.,
van Dongen Maria J.P.,
Voorter Christina E.M.,
Bloemendal Hans,
de Jong Wilfried W.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81113-e
Subject(s) - deamidation , crystallin , chemistry , biochemistry , enzyme
Bovine and human αB‐crystallin undergo deamidation upon aging in the lens. In bovine αB‐crystallin, the specific site of dearnidation 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 glyeyl 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.