Degree of heterogeneity of binding specificities of antibodies to the phenylarsonate group that share a common idiotype.
Degree of heterogeneity of binding specificities of antibodies to the phenylarsonate group that share a common idiotype.
复制标题
具有共同独特型的苯胂酸基团抗体的结合特异性的异质性程度。
DOI：
10.1016/0161-5890(82)90190-0
复制
发表时间：
1982
影响因子：
3.6
通讯作者：
Nisonoff,A
中科院分区：
文献类型：
--
作者：
Kresina,TF;Rosen,SM;Nisonoff,A
我们研究了表达主要独特型(CRIA)的杂交瘤产物(HP)的微观异质性，这些杂交瘤产物与抗对偶氮苯基砷酸盐(Ar)半抗原群的A/J抗体相关。所研究的性质是对苯基取代基的亲和力和各种HP结合部位的良好专一性。通过测量一系列相关半抗原的相对亲和力来探讨其良好的特异性。研究发现，尽管存在变异，但CRIA+HP的抗原结合部位在亲和力和细微的特异性上有很强的相似性。对偶氮苯磺酸-N-~3H-乙酰基-L-酪氨酸的亲和力范围为0.41×10~6−2.2×10~6M−~1。在所有情况下，第二环结构(苯或组氨酸)和偶氮基的加入都大大提高了结合亲和力。幽门螺杆菌与组氨酸的阿山梨酸酯或阿散尼酸衍生物的亲和力有一定差异。然而，在CRIA的常规试验中，两种最强的Hp实际上是彼此相同的，它们诱导的A/J抗Ar抗体具有良好的特异性。结合以往关于氨基酸序列和血清学性质的数据，结果表明，尽管CRI成员具有微观异质性，但它们在结构和半抗原结合特异性上密切相关。
We have investigated the microheterogeneity of hybridoma products (HP) expressing the major idiotype (CRIA) associated with A/J antibodies to thep-azophenylarsonate (Ar) hapten group. The properties investigated were affinity for a phenylarsonate derivative and the fine specificity of the combining sites of the various HP. The fine specificity was approached by measuring relative affinities for a series of related haptens. It was found that, although variations exist, there are strong similarities in affinities and fine specificities of the antigen-binding sites of CRIA+HP. The range of affinities for (p-azobenzenearsonic acid)-N-3H-acetyl-l-tyrosine was 0.41 × 106−2.2 × 106M−1. In all cases the addition of a second ring structure (benzene or histidine) and an azo group greatly increased the binding affinity. Some differences in fine specificity among the HP were seen with respect to affinities foro-arsanilate or the arsanilate derivative of histidine. However, the two HP which are the strongest inhibitors in the conventional assay for CRIAwere virtually identical to one another and to induced A/J anti-Ar antibodies in their fine specificities. Together with previous data on amino acid sequences and serological properties, the results indicate that, despite their microheterogeneity, members of the CRIAfamily are closely related in structure and hapten-binding specificity.