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SUPRAMOLECULAR STRUCTURE OF THE MAMMALIAN LENS

哺乳动物晶状体的超分子结构

基本信息

批准号：
3263330
负责人：
RANDOLPH V. LEWIS
金额：
$ 6.48万
依托单位：
UNIVERSITY OF WYOMING
依托单位国家：
美国
项目类别：
财政年份：
1987
资助国家：
美国
起止时间：
1987-08-01 至 1991-07-31
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/3263330
关键词：
calcium chemical aggregate chemical association chemical cleavage chemical structure chromatography chromophore cow crosslink fluorescent dye /probe ionic strengths lens proteins light scattering physical chemical interaction polymers sodium chloride surface property

项目摘要

It has recently been demonstrated that the transparency of the mammalian lens is apparently due to short range order among the major proteins of the lens, the crystallins. An understanding of the nature of this order is an essential step in obtaining a molecular description of cataract formation (in which this order is disrupted). The major objective of this research is to describe intermolecular interactions between bovine lens crystallins in the form of a two dimensional spatial map of binary protein proximity relationships. This map will be generated by a systematic series of measurements employing three crystallin fractions. The potential existence of crystallin/crystallin interactions will be addressed within both homogeneous crystallin solutions and in all possible binary mixtures of crystallins as a function of protein concentration. The functional significance of any interactions detected will be evaluated based on the observation of the onset of increasing optical transparency seen at high protein concentrations in lens protein extracts. The selection of the experimental methods to be used is based on a desire to minimize perturbation of protein surfaces and a need to make measurements over an unusually wide range of protein concentrations. On this basis, the techniques of dynamic light scattering, chemical crosslinking and fluorescence energy transfer have been chosen to examine crystallin/crystallin interactions. The effect of calcium and sodium chloride will also be explored because of the known effects of these agents on the aggregation of crystallins. The resulting supra-molecular description of the lens in terms of the relative topological locations of the crystallins will then serve as a future framework within which to study cataract related phenomena.

最近的研究表明，哺乳动物的透镜显然是由于短程秩序之间的透镜的主要蛋白质，晶体蛋白。了解这一命令的性质是获得一个白内障形成的分子描述（其中该顺序是中断）。本研究的主要目的是描述牛透镜蛋白分子间相互作用二进制蛋白质邻近度的二维空间图的形式关系。这张地图将由一个系统的系列使用三种晶体蛋白组分的测量。的晶体蛋白/晶体蛋白相互作用的潜在存在将是在均质晶体蛋白溶液和所有晶体蛋白的可能二元混合物作为蛋白质的函数浓度. 任何互动的功能意义将根据观察到的发作情况进行评价在高蛋白质含量下，透镜蛋白提取物中的浓度。的选择使用的实验方法是基于希望最小化蛋白质表面的扰动和需要，在异常广泛的蛋白质范围内进行测量浓度的在此基础上，散射、化学交联和荧光能量转移被选择来检查晶状体蛋白/晶状体蛋白相互作用。钙和氯化钠的影响也将探讨由于这些试剂对聚集的已知影响晶体蛋白由此产生的超分子描述的透镜的相对拓扑位置晶体蛋白将作为未来的框架，研究白内障相关现象。