Complete amino acid sequence of light chain variable regions derived from five monoclonal anti-p-azophenylarsonate antibodies differing with respect to a crossreactive idiotype.
Complete amino acid sequence of light chain variable regions derived from five monoclonal anti-p-azophenylarsonate antibodies differing with respect to a crossreactive idiotype.
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源自交叉反应独特型方面不同的五种单克隆抗对偶氮苯胂酸抗体的轻链可变区的完整氨基酸序列。
DOI：
10.1073/pnas.78.12.7679
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发表时间：
1981
影响因子：
11.1
通讯作者：
Capra,JD
中科院分区：
文献类型：
--
作者：
Siegelman,M;Capra,JD
A/J 小鼠中诱导的对偶氮苯胂半抗原的抗体反应为详细检查可遗传的交叉反应独特型及其精细结构和血清学分析提供了模型系统。虽然早期的研究使用血清反应的明显同质性进行结构研究，但随着单克隆抗体的开发，对胂酸盐独特型系统的更全面的了解成为可能，这些单克隆抗体在这些决定因素方面有所不同。选择五种单克隆抗体进行完整的氨基酸序列分析，其中四种交叉反应独特型阳性，一种交叉反应独特型阴性。这里列出了这些分子的轻链可变区的序列。数据表明单克隆轻链与血清轻链存在相当大的序列差异。然而，无论母体分子的独特型特征如何，单克隆轻链之间都存在显着程度的同源性。尽管在整个可变区中存在明显的微小变化，但所有这些抗胂酸盐抗体的轻链之间的连接区是相同的。在第三高变区中的位置 92 和 93 处发现了特别值得注意的变化焦点。讨论了该区域在轻链对胂酸盐交叉反应独特型的贡献中的可能作用。这些数据与抗胂酸单克隆轻链源自特定 J kappa 基因片段与单个种系 V kappa 基因片段的连接的概念一致。这些编码片段可能进一步受到各种体细胞改变的影响，从而产生最终蛋白质产物中发现的适度序列多样性。
The induced antibody response to the hapten p-azophenylarsonate in the A/J mouse has provided a model system for the detailed examination of a heritable crossreactive idiotype and its fine structural and serologic analysis. While earlier studies used to apparent homogeneity in the serum response for structural studies, a more complete understanding of the arsonate idiotypic system became possible with the development of monoclonal antibodies differing with respect to these determinants. Five monoclonal antibodies, four crossreactive idiotype positive and one crossreactive idiotype negative, were selected for complete amino acid sequence analysis. The sequences of the light chain variable regions of these molecules are presented here. The data indicate considerable sequence divergence of the monoclonal light chains from the serum light chains. However, there is a striking degree of homology among the monoclonal light chains regardless of the idiotype character of the parent molecule. Although minor variations are apparent throughout the variable regions, the joining regions are identical among light chains in all of these anti-arsonate antibodies. A particularly notable focus of variation is found at positions 92 and 93 in the third hypervariable region. The possible role of this region in the contribution of the light chain to the arsonate crossreactive idiotype is discussed. These data are consistent with the concept that the anti-arsonate monoclonal light chains originate from the joining of a specific J kappa gene segment to a single germ-line V kappa gene segment. These coding segments are likely further subject to a variety of somatic alterations that generate the modest sequence diversity found among the final protein products.