Proton nuclear magnetic resonance studies of human immunoglobulins: conformation of the hinge region of the IgG1 immunoglobulin.
Proton nuclear magnetic resonance studies of human immunoglobulins: conformation of the hinge region of the IgG1 immunoglobulin.
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人免疫球蛋白的质子核磁共振研究：IgG1 免疫球蛋白铰链区的构象。
DOI：
10.1021/bi00563a030
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发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
Shimizu,A
中科院分区：
文献类型：
--
作者：
Arata,Y;Honzawa,M;Shimizu,A
摘要：利用位于铰链区的His-224作为内置的质子核磁共振探针，研究了人免疫球蛋白IgG1铰链区的构象。人骨髓瘤免疫球蛋白G1OGO和YOT以及人多克隆免疫球蛋白及其Fab和F(ab‘)2片段用于His-224信号的归属。比较了完整抗体和片段的His-224的滴定行为。结果表明，完整的Ig G和F(ab‘)2片段的滴定曲线与小肽中组氨酸残基的滴定曲线非常相似。相反，Fab片段给出的滴定曲线与完整的Ig G和F(ab‘)2片段的滴定曲线截然不同。结论：(1)在完整的IgG1中，铰链肽完全暴露在溶剂中，并表现出比IgG1更快的内部运动
Yoji Arala,* Mayumi Honzawa, and Akira Shimizu abstract: The conformationof the hinge region of the human IgGl immunoglobulin has been investigated by making use of His-224 in the hinge region as a built-in proton nuclear magnetic resonance (NMR) probe. Human myeloma IgGl («) proteins Ogo and Yot and human polyclonal IgG were used along with their Fab and F (ab') 2 fragments for the assignment of the His-224 signals. The titration behavior of His-224 of the intactIgG and the fragments was compared. It was shown that the titration curves for the intact IgG and the F (ab') 2 fragments are identical and quite similar to those for the histidine residue in small peptides. By contrast, the Fab fragments give titration curves which are quite different from those for the intact IgG and the F (ab') 2 fragments. Conclu-sions derivedmay be summarized as follows:(1) in the intact IgGl, the hinge peptide is fully exposed to the solvent and exhibits internal motion which is much more rapid than the
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