Resistance of α-crystallin quaternary structure to UV irradiation |
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Authors: | A. V. Krivandin K. O. Muranov F. Yu. Yakovlev N. B. Poliansky L. A. Wasserman M. A. Ostrovsky |
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Affiliation: | (1) Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia |
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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). |
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Keywords: | α -crystallin quaternary structure UV radiation small-angle X-ray scattering |
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