α-晶状体蛋白四级结构对紫外线照射的抗性。

Resistance of alpha-crystallin quaternary structure to UV irradiation.

作者信息

Krivandin A V, Muranov K O, Yakovlev F Yu, Poliansky N B, Wasserman L A, Ostrovsky M A

机构信息

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.

出版信息

Biochemistry (Mosc). 2009 Jun;74(6):633-42. doi: 10.1134/s0006297909060078.

DOI:10.1134/s0006297909060078

PMID:19645668

Abstract

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).

摘要

通过小角X射线散射、凝胶渗透色谱法、电泳、吸收光谱和荧光光谱以及差示扫描量热法，研究了紫外线辐射（波长>260nm）对溶液中牛α-晶状体蛋白的损伤作用。所得结果表明，即使α-晶状体蛋白寡聚体内大量亚基受到损伤，也不会导致其四级结构发生显著重排、寡聚体聚集或溶解性丧失。由于其四级结构具有高抗性，α-晶状体蛋白能够防止不稳定蛋白质（尤其是γ-和β-晶状体蛋白）聚集，从而在动物的整个生命过程中维持晶状体的透明度（α-晶状体蛋白的伴侣样功能）。