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Age‐dependent deamidation of chicken αA‐crystallin
Author(s) -
Voorter Christina E.M.,
Roersma Eric S.,
Bloemendal Hans,
de Jong Wilfried W.
Publication year - 1987
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(87)80935-3
Subject(s) - deamidation , cyanogen bromide , crystallin , peptide , asparagine , chemistry , biochemistry , lysine , aspartic acid , peptide sequence , amino acid , cleavage (geology) , enzyme , gene , biology , paleontology , fracture (geology)
The major posttranslational modification product of αA‐crystallin from chicken eye lenses has one more negative charge than the corresponding primary gene product. These polypeptides were compared by peptide mapping after tryptic digestion and cyanogen bromide cleavage, and the charge difference could be located in a peptide, comprising residues 146–150 of the amino acid sequence of αA‐crystallin. Subsequent enzymatic hydrolysis with aminopeptidase showed that asparagine at position 149 of the primary gene product is replaced by aspartic acid. Two‐dimensional gel electrophoresis of total lens homogenates from chickens of different ages revealed an age‐dependent increase of the deamidated αA‐subunit.