Degradation of γD- and γs-Crystallins in Human Lenses
- 1 December 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 253 (2), 288-294
- https://doi.org/10.1006/bbrc.1998.9728
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Sequence Analysis of βA3, βB3, and βA4 Crystallins Completes the Identification of the Major Proteins in Young Human LensJournal of Biological Chemistry, 1997
- Characterization of Three Isoforms of a 9kDa γD-Crystallin Fragment Isolated From Human LensesExperimental Eye Research, 1996
- Covalent Modification at the C-Terminal End of a 9 kDa γD-Crystallin Fragment in Human LensesExperimental Eye Research, 1994
- Identification of a γs-Crystallin Fragment in Human LensesExperimental Eye Research, 1993
- Identification of a 9 kDa γ-crystallin fragment in human lensesExperimental Eye Research, 1992
- High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis.Proceedings of the National Academy of Sciences, 1991
- Immunochemical characterization of the major low molecular weight polypeptide (10K) from human cataractous lensesExperimental Eye Research, 1989
- Age-related increase in concentration and aggregation of degraded polypeptides in human lensesExperimental Eye Research, 1988
- Variation in proportion and molecular weight of native crystallins from single human lenses upon aging and formation of nuclear cataractExperimental Eye Research, 1983
- Comparison of the 10 000 and 43 000 dalton polypeptide populations isolated from the water soluble and insoluble fractions of human cataractous lensesExperimental Eye Research, 1979