The Interaction of Dinitrobenzene Derivatives with Bovine Serum Albumin1,2
The Interaction of Dinitrobenzene Derivatives with Bovine Serum Albumin1,2
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二硝基苯衍生物与牛血清白蛋白的相互作用1,2
DOI：
10.1021/ja01114a017
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发表时间：
1953
影响因子：
15
通讯作者：
H. Eisen
中科院分区：
文献类型：
--
作者：
M. E. Carsten;H. Eisen
研究了一系列离子和非离子取代的2,4 -二硝基苯与牛血清白蛋白在两种温度下的可逆相互作用。它们之间的区别只在于1号碳上的取代基。该系列包括两个2,4 -二硝基苯氨基酸。发现1号碳上取代基的性质大大改变了结合亲和力。用图形得到了相对结合亲和度，并计算了相互作用能（AH'0）。氯离子抑制牛血清白蛋白对二硝基苯酚的结合，而对二硝基苯胺的结合无抑制作用。二硝基甲苯还能抑制二硝基苯酚的结合。与牛血清白蛋白结合导致e-二硝基苯-氨基己酸、二硝基苯胺和二硝基苯酚的吸收光谱发生变化。无机和有机离子与血清白蛋白的相互作用已被广泛研究。然而，直到最近中性有机分子的结合才引起人们的注意。我们研究了牛血清白蛋白与一系列离子和非离子取代的2,4 -二硝基苯的可逆相互作用，它们只是在碳1上的取代基不同。该系列包括一些2,4 -二硝基苯（DNP）氨基酸。所研究的化合物使评估各种取代基对结合的贡献成为可能，特别是获得离子对结合的贡献的信息。离子化合物在非离子同系物存在下的结合使得对结合位点的特异性有了一些了解成为可能。此外，从免疫学的角度来看，取代的2,4 -二硝基苯是相当有趣的。这些化合物中的一些，在适当的条件下，引起广泛的过敏反应。这些化合物与血清白蛋白的相互作用为解释这些生物现象提供了基础，并且与2,4 -二硝基苯基特异性抗体相关的相互作用特别有趣。后一个问题正在本实验室进行研究。本文记录了以下2,4 -二硝基苯衍生物-的结合测量
The reversible interaction of a series of ionic and non-ionic substituted 2, 4-dinitrobenzenes with bovine serum albumin has been studied attwo temperatures. They differed from each other only in the substituent at carbon one. Included in the series were two 2, 4-dinitrophenyl amino acids. The nature of the substituent at carbon one was found to modify consider-ably the binding affinity. Relative binding affinities were obtained graphically and energies of interaction (AH'0) computed. Chloride ion inhibits the binding of dinitrophenol by bovine serum albumin but not that of dinitroaniline. Dinitrotoluene also inhibits binding of dinitrophenol. Binding to bovine serum albumin results in shifts in the absorption spectra of e-dinitrophenyl-aminocaproic acid, dinitroaniline and dinitrophenol.The interactions of inorganic and organic ions with serum albumins havebeen studied extensively. Little attention, however, has been given until very recently to the binding of neutral organic mole-cules. 3 We have studied the reversible interactions of bovine serum albumin with a series of ionic and non-ionic substituted 2, 4-dinitrobenzenes which differ only in the substituent at carbon one. In-cluded in this series were some 2, 4-dinitrophenyl (DNP) amino acids. The compounds studied made it possible to evaluatethe contribution of the various substituents to the binding and, in par-ticular, to obtaininformation on the ionic con-tribution to the binding. The binding of an ionic compound in the presence of a non-ionic homolog has made it possible to gain some insight into the specificity of binding sites. Furthermore, substituted 2, 4-dinitrobenzenes are of considerable interest from an immunologic view-point. Some of these compounds, under appropri-ate conditions, give rise to a wide range of allergic reactions. 4 The interaction of these compounds with serum albumin provides a basis for interpreting some of these biological phenomena5 and is of particular interest in relation to corresponding interactions involving antibodies specific for the 2, 4-dinitrophenyl group. The latter problem is under study in this Laboratory. The present paper records measurements of the binding of the following 2, 4-dinitrobenzene deriva-