Resistance of alpha-crystallin quaternary structure to UV irradiation.
The damaging effect of UV radiation (lambda > 260 nm) on bovine alpha-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 alpha-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, alpha-crystallin is able to prevent aggregation of destabilized proteins (especially of gamma- and beta-crystallins) and so to maintain lens transparency throughout the life of an animal (the chaperone-like function of alpha-crystallin).
Krivandin
A V
AV
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. a.krivandin@sky.chph.ras.ru
Muranov
K O
KO
Yakovlev
F Yu
FY
Poliansky
N B
NB
Wasserman
L A
LA
Ostrovsky
M A
MA
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007904:Lens Cortex, Crystalline / Q000737:chemistry; D011489:Protein Denaturation; D020836:Protein Structure, Quaternary / Q000528:radiation effects*; D053838:Scattering, Small Angle; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D014466:Ultraviolet Rays / Q000009:adverse effects*; D038201:alpha-Crystallins / Q000737:chemistry* / Q000302:isolation & purification / Q000528:radiation effects
D038201:alpha-Crystallins