Conservation among vertebrate immunoglobulin chains detected by antibodies to a synthetic joining segment peptide.
Conservation among vertebrate immunoglobulin chains detected by antibodies to a synthetic joining segment peptide.
复制标题
通过合成连接片段肽的抗体检测脊椎动物免疫球蛋白链之间的保守性。
DOI：
10.1016/0006-291x(87)91021-7
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发表时间：
1987
影响因子：
3.1
通讯作者：
Marchalonis,JJ
中科院分区：
文献类型：
--
作者：
Schluter,SF;Rosenshein,IL;Hubbard,RA;Marchalonis,JJ
我们使用针对对应于人T细胞受体基因的整个J β的合成肽序列产生的亲和纯化抗体来筛选人、小鼠和其他脊椎动物的血清，以确定交叉反应分子的存在。几乎没有发现游离α β异二聚体的证据，但抗体与许多脊椎动物物种的轻链反应，包括人和小鼠的特征性骨髓瘤蛋白。一些脊椎动物目，特别是鸟类，缺乏与J β交叉反应的多肽链，但在原始脊椎动物如加拉帕戈斯鲨鱼（Carcharhinus galapagensis）中存在可检测的决定簇。除了与纯化轻链的强交叉反应外，人重链与抗体的反应较弱。交叉反应与变性免疫球蛋白的序列相关，与游离肽可重复。这些结果确立了T细胞受体β链与免疫球蛋白链的相似性，并支持J区序列不仅在哺乳动物免疫球蛋白和T细胞受体中，而且在脊椎动物进化中是保守的结论。
We used affinity purified antibodies produced against a synthetic peptide sequence corresponding to the entire J β of a human T cell receptor gene to screen sera of man, mouse and other vertebrates to determine the presence of cross-reactive molecules. Little evidence for free α β heterodimers was found, but the antibody reacted with light chains of many vertebrate species, including characterized myeloma proteins of man and mouse. Some vertebrate orders, notably Aves, lacked polypeptide chains cross-reactive with J β, but detectable determinants occurred in primitive vertebrates such as the galapagos shark (Carcharhinus galapagensis). In addition to the strong cross-reaction with purified light chains, human heavy chains reacted weakly with the antibody. The cross-reaction correlated with the sequence of the denatured immunoglobulins and was inhibitable with free peptide. These results establish the similarity of T cell receptor β chains to immunoglobulin chains and support the conclusion that J region sequences were conserved, not only within mammalian immunoglobulins and T cell receptors, but in vertebrate evolution.