Magnetic resonance of a monoclonal anti-spin-label antibody
Magnetic resonance of a monoclonal anti-spin-label antibody
复制标题
单克隆抗自旋标记抗体的磁共振
DOI：
10.1021/bi00301a016
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发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
H. Mcconnell
中科院分区：
文献类型：
--
作者：
J. Anglister;T. Frey;H. Mcconnell
Jacob Anglister, Tom Frey, and Harden M. McConnell*摘要：在没有和存在特定自旋标记二硝基苯半抗原的情况下，记录了非克隆Fab抗体片段的核磁共振谱。差异光谱显示在结合位点区域存在11-12个芳香氨基酸。通过对该杂交瘤抗体的选择性氘化，这些氨基酸被鉴定为三个色氨酸、六个或七个酪氨酸、一个苯丙氨酸和一个组氨酸。差异光谱也被记录，依赖于环电流a抗体分子在防御感染中起着至关重要的作用。当面对几乎任何外来分子时，免疫系统都能够产生高亲和力和高度特异性的抗体蛋白。多年来，抗体特异性的结构基础一直是免疫化学关注的主要问题之一。对抗体序列的统计分析表明，这种特异性是由相对较短的片段决定的，即高变区（Wu & Kabat, 1970）。晶体学研究表明，结合位点是由这些高变区形成的。
Jacob Anglister,* Tom Frey, and Harden M. McConnell* abstract: The nuclear magnetic resonance spectra of mo-noclonal Fab antibody fragments have been recorded in the absence and presence of a specific spin-label dinitrophenyl hapten. The difference spectra reveal the presence of 11-12 aromatic amino acids in the region of the combining site. By selective deuteration of this hybridoma antibody, these amino acids have been identified as three tryptophans, six or seven tyrosines, one phenylalanine, and one histidine. Difference spectra have also been recorded that depend on ring-current-A-ntibody molecules play a crucial role in defense against infection. When confronted by almost any foreign molecule, the immune system is able to produce antibody proteins of high affinity and exquisite specificity. Thestructural basis of an-tibody specificity has been one of the major concerns of im-munochemistry for many years. Statistical analysis of antibody sequences shows that this specificity is determined by relatively short segments, the hypervariable regions (Wu & Kabat, 1970). Crystallographic studies reveal that the combining sites are formed by these hypervariable regions [for recent reviews,