STRUCTURE OF ANTIBODIES WITH SHARED IDIOTYPY - COMPLETE SEQUENCE OF HEAVY-CHAIN VARIABLE REGIONS OF 2 IMMUNOGLOBULIN-M ANTI-GAMMA GLOBULINS
STRUCTURE OF ANTIBODIES WITH SHARED IDIOTYPY - COMPLETE SEQUENCE OF HEAVY-CHAIN VARIABLE REGIONS OF 2 IMMUNOGLOBULIN-M ANTI-GAMMA GLOBULINS
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DOI：
10.1073/pnas.71.10.4032
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发表时间：
1974-01-01
影响因子：
11.1
通讯作者：
KEHOE, JM
中科院分区：
文献类型：
--
作者：
CAPRA, JD;KEHOE, JM
已测定两种不同免疫球蛋白M抗γ球蛋白分子的重链可变区的完整氨基酸序列。这些来自不同人类患者的蛋白质已被独立地证明具有独特型特异性。对于其重链可变区的整个长度，仅8个序列差异是可辨别的。其中五个差异发生在高变区之外，而三个差异发生在高变区之内。将这些抗γ球蛋白分子与目前可用于免疫球蛋白的七种人VH III可变区序列进行比较，但没有已知的抗体活性，结果表明，这两种独特的相似抗体和这七种蛋白质之间的绝大多数序列差异局限于高变区。和结合位点特异性，因为它们涉及免疫球蛋白分子的可变区。在很大程度上，这些属性现在似乎是可变区相同结构属性的反映。
The complete amino acid sequence of the heavy chain variable regions of two different molecules of immunoglobulin M anti-gamma globulin has been determined. These proteins, from different human patients, had independently been shown to share idiotypic specificity. Only eight sequence differences were discernible for the entire length of their heavy chain variable regions. Five of the differences occurred outside hypervariable regions, while three were placeable within such regions. A comparison of these molecules of anti-gamma globulin with the seven human VHIII variable region sequences presently available for immunoglobulins without known antibody activity showed that the great majority of sequence differences between the two idiotypically similar antibodies and these seven proteins were confined to hypervariable regions.This study illustrates in precise terms a convergence of the distinct immunological properties of idiotypy, hypervariable region structure, and combining site specificity as they relate to the variable region of the immunoglobulin molecule. To a great degree these properties now appear to be a reflection of the same structural attributes of the variable region.