Age‐dependent deamidation of chicken αA‐crystallin
- 14 September 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 221 (2), 249-252
- https://doi.org/10.1016/0014-5793(87)80935-3
Abstract
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.Keywords
This publication has 15 references indexed in Scilit:
- Some aspects of the phosphorylation of α‐crystallin AEuropean Journal of Biochemistry, 1986
- cAMP-dependent phosphorylation of bovine lens alpha-crystallin.Proceedings of the National Academy of Sciences, 1985
- Ratites as oldest offshoot of avian stem—evidence from α-crystallin A sequencesNature, 1984
- Primary structures of the α‐crystallin A chains of twenty‐eight mammalian species, chicken and frogEuropean Journal of Biochemistry, 1984
- The Lens: Development, Proteins, Metabolism and CataractPublished by Elsevier ,1984
- Lens Proteins and AgingJournal of Gerontology, 1983
- Aging of protein molecules: lens crystallins as a model systemTrends in Biochemical Sciences, 1981
- The Amino‐Acid Sequences of the α‐Crystallin A Chains of Red Kangaroo and Virginia OpossumEuropean Journal of Biochemistry, 1976
- Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageingNature, 1975
- Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide GroupsNature, 1966