Site‐specific racemization in aging α‐crystallin
- 20 August 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 269 (1) , 109-112
- https://doi.org/10.1016/0014-5793(90)81131-7
Abstract
Of all aspartyl residues in bovine αA-crystallin, only Asp-151 exhibits pronounced racemization. Asp-151 is also one of the sites where peptide bond cleavage occurs in in vivo aging αA-crystallin. This aspartyl residue is followed by an alanyl residue and resides in a flexible carboxyl terminal extension of α-crystallin. Both in vivo and in vitro racemization studies indicate that the pronounced and site-specific racemization of Asp-151 proceeds via formation of a succinimide intermediate. The in vivo racemization of aspartyl residues in αA-crystallin is discussed with regard to the proposed tertiary structure of α-crystallin.Keywords
This publication has 25 references indexed in Scilit:
- Tertiary Structure Is a Principal Determinant to Protein DeamidationScience, 1988
- Protein distribution patterns in concentric layers from single bovine lenses: changes with development and ageingCurrent Eye Research, 1988
- Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteinsInternational Journal of Peptide and Protein Research, 1987
- Domain structure and evolution in α‐crystallins and small heat‐shock proteinsFEBS Letters, 1985
- Primary structures of the α‐crystallin A chains of twenty‐eight mammalian species, chicken and frogEuropean Journal of Biochemistry, 1984
- Aspartic acid racemisation in the human lens during ageing and in cataract formationNature, 1977
- Aspartic acid racemisation in dentine as a measure of ageingNature, 1976
- Intracellular Degradation and Deamidation of α‐Crystallin SubunitsEuropean Journal of Biochemistry, 1976
- Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageingNature, 1975
- The Amino‐Acid Sequence of the αA2 Chain of Bovine α‐CrystallinEuropean Journal of Biochemistry, 1973