Lawson E Q, Schubert C F, Lewis R V, Middaugh C R
J Biol Chem. 1981 Jul 10;256(13):6523-5.
Apparent thermodynamic parameters for the process of solubilization of the five major classes of bovine lens crystallins have been determined by the polyethylene glycol solubility method. Although each purified crystallin fraction displays significant structural heterogeneity as analyzed by high performance liquid chromatography, they behave as homogeneous proteins by the criteria of solubility. Using experimentally determined values for the apparent enthalpy and entropy of solution and the effects of a variety of low molecular weight solutes on crystallin solubility, the five classes can be arranged in order of the polarity of their solid phase intermolecular contacts as follows: gamma, high molecular weight beta greater than low molecular weight beta greater than high molecular weight alpha greater than alpha. Since alpha-crystallin is the major component of the insoluble material in bovine cataract, we suggest that cataract formation may be related to the intrinsic solubility and polarity of the lens crystallins.
已通过聚乙二醇溶解度法测定了牛晶状体中五类主要晶状体蛋白溶解过程的表观热力学参数。尽管通过高效液相色谱分析,每个纯化的晶状体蛋白组分都显示出显著的结构异质性,但按照溶解度标准,它们表现为均质蛋白。利用实验测定的溶液表观焓和熵值以及各种低分子量溶质对晶状体蛋白溶解度的影响,这五类蛋白可按其固相分子间接触极性的顺序排列如下:γ、高分子量β大于低分子量β大于高分子量α大于α。由于α-晶状体蛋白是牛白内障中不溶性物质的主要成分,我们认为白内障的形成可能与晶状体蛋白的固有溶解度和极性有关。