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- Title
Resistance of α-crystallin quaternary structure to UV irradiation.
- Authors
Krivandin, A. V.; Muranov, K. O.; Yakovlev, F. Yu.; Poliansky, N. B.; Wasserman, L. A.; Ostrovsky, M. A.
- Abstract
The damaging effect of UV radiation (λ > 260 nm) on bovine α-crystallin in solution was studied by small-angle X-ray scattering, gel permeation chromatography, electrophoresis, absorption and fluorescence spectroscopy, and differential scanning calorimetry. The results obtained show that damage to even a large number of subunits within an α-crystallin oligomer does not cause significant rearrangement of its quaternary structure, aggregation of oligomers, or the loss of their solubility. Due to the high resistance of its quaternary structure, α-crystallin is able to prevent aggregation of destabilized proteins (especially of γ- and β-crystallins) and so to maintain lens transparency throughout the life of an animal (the chaperone-like function of α-crystallin).
- Subjects
ULTRAVIOLET radiation; X-ray scattering; GEL permeation chromatography; ELECTROPHORESIS; FLUORESCENCE spectroscopy; OLIGOMERS
- Publication
Biochemistry (00062979), 2009, Vol 74, Issue 6, p633
- ISSN
0006-2979
- Publication type
Article
- DOI
10.1134/S0006297909060078