Adlersberg J B
Ric Clin Lab. 1976 Jul-Sep;6(3):191-205.
The hinge region is a flexible amino acid stretch in the central part of the heavy chains of the IgG and IgA immunoglobulin classes, which links these 2 chains by disulfide bonds. It is rich in cysteine and proline amino acids, extremely variable in amino acid sequence, and has no resemblance to any other immunoglobulin region. The hinges in these 2 classes are compared and contrasted. Such a distinct molecular structure does not exist around the inter-heavy disulfide bonds of the other Ig classes, but a portion of the IgM heavy chain has similar properties to the gamma hinge. This similarity suggests one hypothesis for the genetic origin of the hinge region; data supporting 2 other hypotheses are also presented.
铰链区是IgG和IgA免疫球蛋白类重链中部一段灵活的氨基酸序列，通过二硫键连接两条重链。它富含半胱氨酸和脯氨酸，氨基酸序列变化极大，与其他免疫球蛋白区域毫无相似之处。本文对这两类免疫球蛋白的铰链区进行了比较和对比。其他免疫球蛋白类的重链间二硫键周围不存在如此独特的分子结构，但IgM重链的一部分具有与γ铰链类似的特性。这种相似性为铰链区的基因起源提出了一种假说；同时也给出了支持另外两种假说的数据。
