Xia J Z, Wang Q, Tatarkova S, Aerts T, Clauwaert J
Department of Biochemistry, University of Antwerp, U.I.A., Belgium.
Biophys J. 1996 Nov;71(5):2815-22. doi: 10.1016/S0006-3495(96)79477-8.
Short range order of the crystallins does account for the transparency of the eye lens. To explain the solution structure of this highly concentrated protein solution on a quantitative basis, the hydrodynamic structure and the interparticle interactions of the proteins have to be known. For that purpose, the light scattering of concentrated solutions of alpha-crystallin has been studied. Starting from the detailed knowledge of the solution parameters of alpha-crystallin in diluted solutions, the structure of concentrated solutions up to 360 mg/ml has been studied using light scattering. Our results indicate that subtle changes in the macromolecular structure such as optical anisotropy or structural asymmetry for part of the alpha-crystallins, which results in solute light-scattering heterogeneity, can dramatically increase the light scattering by the alpha-crystallins and cause solution opacity.
晶状体蛋白的短程有序排列确实是晶状体透明的原因。为了定量解释这种高浓度蛋白质溶液的溶液结构，必须了解蛋白质的流体动力学结构和颗粒间相互作用。为此，对α-晶状体蛋白浓缩溶液的光散射进行了研究。从对稀释溶液中α-晶状体蛋白溶液参数的详细了解出发，利用光散射研究了浓度高达360mg/ml的浓缩溶液的结构。我们的结果表明，大分子结构的细微变化，如部分α-晶状体蛋白的光学各向异性或结构不对称性，会导致溶质光散射不均匀性，从而显著增加α-晶状体蛋白的光散射并导致溶液不透明。
